Cell junction organization (Homo sapiens)

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10, 1319, 15, 2516233231222202321727, 3024292, 1116174, 1826523146, 28821126232831cytosolcytosolPARD6G CDH9 Cadherin:CatenincomplexCD151:BP230:BP180:Plectin:Integrin alpha 6 beta 4: LamininParvB/Affixin:Alpha-PixCADM3 CDH18 Laminin-332FBLIM1 VASPCADM3Par3:Par6:aPKCcomplexCDH17 LAMA3 PVRL3 PVRL3 PVRL4 PVRL3 BP230:BP180:Plectin:integrin alpha 6 beta 4:Laminin 332PARVB:alpha actininPVRL1 ACTN1 ARHGEF6Necl-1:Necl-2 transheterodimerPARVA LAMA3 CRB3CDH4 FBLIM1 CDH11 PVRL1 CTNNA1 PARVA:TESK1PVRL2 CDH18 PARVA:PaxillinITGA6(24-1130) ITGB1CDH11 CADM3 CDH6 ACTN1F11R Integrinalpha6:beta4:Plectin:BP180:Laminin-322 complexLAMC2 PARVB PARVA COL17A1(1-1497)LAMC2 PARD3 Classic CadherinPVRL1 CDH3 Ca2+PARVBMLLT4-2LAMA3 PVRL1 MIGFILIN:VASPFLNA ClaudinIntegrinalpha6:beta4:Plectin:BP180 complexLAMB3 FLNC PXNPVRL3 COL17A1(1-1497) ARHGEF6 CDH12 FERMT2ILK Nectin-1:Nectin-4trans heterodimerPVRL2 PVRL4 CDH6 PARD6G CDH7 CDH24 CADM1 COL17A1(1-1497) PVR CADM2 PVRL4 CDH4 CDH2 TESK1 COL17A1(1-1497) VASP ITGB4 ITGB4 CDH10 MPP5PVRCDH3 PVRL3 dimerLAMA3 VE-cadherin Integrin alpha6:beta 4:PlectincomplexCADM3 CDH12 CDH2 PLEC Necl-1:Nectin-3trans heterodimerIntegrin alpha6beta4Rsu-1:Pinch1 complexType IIhemidesmosomeJUP PRKCI Nectin-2 cishomodimerFBLIM1 VE-cadherin Nectin transhomodimerMPP5 PARD6B PINCHCRB3:PALS1:PATJcomplexITGA6(24-1130) LIMS2 PLEC PARD6B CDH1(155-882) CDH8 PVRL1 alpha/beta parvinCDH13 PVRL1ITGA6(24-1130) CADM1 CDH15 PVRL2 RSU1 JAM-A:PAR-aPKCcomplexFBLIM1PVRL3 ILK PARD3 CD151PVRL3LAMB3 PARD6A PVRL3 F11RPVRL2 CTNNA1CADM1 ITGA6(24-1130) PVRL3 INADLILK:Integrin beta-1PRKCI CDH1(155-882) PARVB LAMC2 MLLT4-2 PLECCTNND1ITGB4 FERMT2 CADM3 PVRL3 Cadherintrans-homodimerclaudintrans-homodimerNecl-1:Nectin-1trans heterodimerPVRL1 PLEC Beta-catenin/gammacateninITGB1 COL17A1(1-1497) PLEC Nectin-1 cishomodimerITGB4 PRV:PVRL3 transheterodimerMIG-2:MIGFILINKeratin 5/14PXN CDH9 FilaminCD151 LAMB3 Nectin-3:Necl-2trans heterodimerNectin-4 cishomodimerPVRL4 LAMC2 ITGB4 PLEC LIMS1Afadin:F-actinCOL17A1(1-1497) CDH17 LIMS1 CDH7 Nectin cis-homodimerPLEC PVRL2 Nectin:afadincomplexCDH15 LAMC2 LAMB3 CDH13 PVRL4 LAMA3 ITGA6(24-1130) PVRL3 LIMS1 CADM1CDH10 CRB3 CD151 LAMB3 PINCH-ILK-parvincomplexINADL Migfilin:FilaminA:F-actinITGA6(24-1130) ITGA6(24-1130) MLLT4-2 Necl-1/Necl-2/Necl-3homodimerILKRSU1ITGB4 Nectin-2:PVRL3transheterodimerPARD6A CTNND1 BP230TESK1PVRL1 Necl-1/Necl-2/Necl-3trans homodimerNectinF-actinNectin-1:PVRL3 transheterodimerCDH24 CDH8 PARVAITGB4 19


Description

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Bibliography

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  1. Ebnet K, Aurrand-Lions M, Kuhn A, Kiefer F, Butz S, Zander K, Meyer zu Brickwedde MK, Suzuki A, Imhof BA, Vestweber D.; ''The junctional adhesion molecule (JAM) family members JAM-2 and JAM-3 associate with the cell polarity protein PAR-3: a possible role for JAMs in endothelial cell polarity.''; PubMed Europe PMC Scholia
  2. Dantzig AH, Hoskins JA, Tabas LB, Bright S, Shepard RL, Jenkins IL, Duckworth DC, Sportsman JR, Mackensen D, Rosteck PR.; ''Association of intestinal peptide transport with a protein related to the cadherin superfamily.''; PubMed Europe PMC Scholia
  3. Zhang Y, Tu Y, Gkretsi V, Wu C.; ''Migfilin interacts with vasodilator-stimulated phosphoprotein (VASP) and regulates VASP localization to cell-matrix adhesions and migration.''; PubMed Europe PMC Scholia
  4. Pellissier F, Gerber A, Bauer C, Ballivet M, Ossipow V.; ''The adhesion molecule Necl-3/SynCAM-2 localizes to myelinated axons, binds to oligodendrocytes and promotes cell adhesion.''; PubMed Europe PMC Scholia
  5. Wang X, Fukuda K, Byeon IJ, Velyvis A, Wu C, Gronenborn A, Qin J.; ''The structure of alpha-parvin CH2-paxillin LD1 complex reveals a novel modular recognition for focal adhesion assembly.''; PubMed Europe PMC Scholia
  6. Padhi AK, Banerjee K, Gomes J, Banerjee M.; ''Computational and functional characterization of Angiogenin mutations, and correlation with amyotrophic lateral sclerosis.''; PubMed Europe PMC Scholia
  7. Yamaji S, Suzuki A, Kanamori H, Mishima W, Yoshimi R, Takasaki H, Takabayashi M, Fujimaki K, Fujisawa S, Ohno S, Ishigatsubo Y.; ''Affixin interacts with alpha-actinin and mediates integrin signaling for reorganization of F-actin induced by initial cell-substrate interaction.''; PubMed Europe PMC Scholia
  8. Kaufman L, Yang G, Hayashi K, Ashby JR, Huang L, Ross MJ, Klotman ME, Klotman PE.; ''The homophilic adhesion molecule sidekick-1 contributes to augmented podocyte aggregation in HIV-associated nephropathy.''; PubMed Europe PMC Scholia
  9. Tu Y, Huang Y, Zhang Y, Hua Y, Wu C.; ''A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading.''; PubMed Europe PMC Scholia
  10. Lopez M, Aoubala M, Jordier F, Isnardon D, Gomez S, Dubreuil P.; ''The human poliovirus receptor related 2 protein is a new hematopoietic/endothelial homophilic adhesion molecule.''; PubMed Europe PMC Scholia
  11. Yamagata M, Weiner JA, Sanes JR.; ''Sidekicks: synaptic adhesion molecules that promote lamina-specific connectivity in the retina.''; PubMed Europe PMC Scholia
  12. Dong X, Xu F, Gong Y, Gao J, Lin P, Chen T, Peng Y, Qiang B, Yuan J, Peng X, Rao Z.; ''Crystal structure of the V domain of human Nectin-like molecule-1/Syncam3/Tsll1/Igsf4b, a neural tissue-specific immunoglobulin-like cell-cell adhesion molecule.''; PubMed Europe PMC Scholia
  13. Hopkinson SB, Jones JC.; ''The N terminus of the transmembrane protein BP180 interacts with the N-terminal domain of BP230, thereby mediating keratin cytoskeleton anchorage to the cell surface at the site of the hemidesmosome.''; PubMed Europe PMC Scholia
  14. de Pereda JM, Lillo MP, Sonnenberg A.; ''Structural basis of the interaction between integrin alpha6beta4 and plectin at the hemidesmosomes.''; PubMed Europe PMC Scholia
  15. Mishima W, Suzuki A, Yamaji S, Yoshimi R, Ueda A, Kaneko T, Tanaka J, Miwa Y, Ohno S, Ishigatsubo Y.; ''The first CH domain of affixin activates Cdc42 and Rac1 through alphaPIX, a Cdc42/Rac1-specific guanine nucleotide exchanging factor.''; PubMed Europe PMC Scholia
  16. LaLonde DP, Brown MC, Bouverat BP, Turner CE.; ''Actopaxin interacts with TESK1 to regulate cell spreading on fibronectin.''; PubMed Europe PMC Scholia
  17. Lorenz S, Vakonakis I, Lowe ED, Campbell ID, Noble ME, Hoellerer MK.; ''Structural analysis of the interactions between paxillin LD motifs and alpha-parvin.''; PubMed Europe PMC Scholia
  18. Rosenberger G, Jantke I, Gal A, Kutsche K.; ''Interaction of alphaPIX (ARHGEF6) with beta-parvin (PARVB) suggests an involvement of alphaPIX in integrin-mediated signaling.''; PubMed Europe PMC Scholia
  19. Michel D, Arsanto JP, Massey-Harroche D, Béclin C, Wijnholds J, Le Bivic A.; ''PATJ connects and stabilizes apical and lateral components of tight junctions in human intestinal cells.''; PubMed Europe PMC Scholia
  20. Masuda M, Yageta M, Fukuhara H, Kuramochi M, Maruyama T, Nomoto A, Murakami Y.; ''The tumor suppressor protein TSLC1 is involved in cell-cell adhesion.''; PubMed Europe PMC Scholia
  21. Kakunaga S, Ikeda W, Itoh S, Deguchi-Tawarada M, Ohtsuka T, Mizoguchi A, Takai Y.; ''Nectin-like molecule-1/TSLL1/SynCAM3: a neural tissue-specific immunoglobulin-like cell-cell adhesion molecule localizing at non-junctional contact sites of presynaptic nerve terminals, axons and glia cell processes.''; PubMed Europe PMC Scholia
  22. Tu Y, Wu S, Shi X, Chen K, Wu C.; ''Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation.''; PubMed Europe PMC Scholia
  23. Takahashi K, Nakanishi H, Miyahara M, Mandai K, Satoh K, Satoh A, Nishioka H, Aoki J, Nomoto A, Mizoguchi A, Takai Y.; ''Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein.''; PubMed Europe PMC Scholia
  24. Hannigan GE, Leung-Hagesteijn C, Fitz-Gibbon L, Coppolino MG, Radeva G, Filmus J, Bell JC, Dedhar S.; ''Regulation of cell adhesion and anchorage-dependent growth by a new beta 1-integrin-linked protein kinase.''; PubMed Europe PMC Scholia
  25. Mueller S, Wimmer E.; ''Recruitment of nectin-3 to cell-cell junctions through trans-heterophilic interaction with CD155, a vitronectin and poliovirus receptor that localizes to alpha(v)beta3 integrin-containing membrane microdomains.''; PubMed Europe PMC Scholia
  26. Ebnet K, Suzuki A, Horikoshi Y, Hirose T, Meyer Zu Brickwedde MK, Ohno S, Vestweber D.; ''The cell polarity protein ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM).''; PubMed Europe PMC Scholia
  27. Sterk LM, Geuijen CA, Oomen LC, Calafat J, Janssen H, Sonnenberg A.; ''The tetraspan molecule CD151, a novel constituent of hemidesmosomes, associates with the integrin alpha6beta4 and may regulate the spatial organization of hemidesmosomes.''; PubMed Europe PMC Scholia
  28. Koster J, Geerts D, Favre B, Borradori L, Sonnenberg A.; ''Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly.''; PubMed Europe PMC Scholia
  29. Dougherty GW, Jose C, Gimona M, Cutler ML.; ''The Rsu-1-PINCH1-ILK complex is regulated by Ras activation in tumor cells.''; PubMed Europe PMC Scholia
  30. Lemmers C, Médina E, Delgrossi MH, Michel D, Arsanto JP, Le Bivic A.; ''hINADl/PATJ, a homolog of discs lost, interacts with crumbs and localizes to tight junctions in human epithelial cells.''; PubMed Europe PMC Scholia
  31. Reymond N, Fabre S, Lecocq E, Adelaïde J, Dubreuil P, Lopez M.; ''Nectin4/PRR4, a new afadin-associated member of the nectin family that trans-interacts with nectin1/PRR1 through V domain interaction.''; PubMed Europe PMC Scholia
  32. Ali J, Liao F, Martens E, Muller WA.; ''Vascular endothelial cadherin (VE-cadherin): cloning and role in endothelial cell-cell adhesion.''; PubMed Europe PMC Scholia
  33. Fontao L, Favre B, Riou S, Geerts D, Jaunin F, Saurat JH, Green KJ, Sonnenberg A, Borradori L.; ''Interaction of the bullous pemphigoid antigen 1 (BP230) and desmoplakin with intermediate filaments is mediated by distinct sequences within their COOH terminus.''; PubMed Europe PMC Scholia
  34. Hülsken J, Birchmeier W, Behrens J.; ''E-cadherin and APC compete for the interaction with beta-catenin and the cytoskeleton.''; PubMed Europe PMC Scholia
  35. Dickson KA, Kang DK, Kwon YS, Kim JC, Leland PA, Kim BM, Chang SI, Raines RT.; ''Ribonuclease inhibitor regulates neovascularization by human angiogenin.''; PubMed Europe PMC Scholia

History

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CompareRevisionActionTimeUserComment
114723view16:20, 25 January 2021ReactomeTeamReactome version 75
113167view11:23, 2 November 2020ReactomeTeamReactome version 74
112395view15:33, 9 October 2020ReactomeTeamReactome version 73
101299view11:18, 1 November 2018ReactomeTeamreactome version 66
100836view20:49, 31 October 2018ReactomeTeamreactome version 65
100377view19:24, 31 October 2018ReactomeTeamreactome version 64
99924view16:08, 31 October 2018ReactomeTeamreactome version 63
99479view14:40, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99133view12:40, 31 October 2018ReactomeTeamreactome version 62
94016view13:51, 16 August 2017ReactomeTeamreactome version 61
93635view11:29, 9 August 2017ReactomeTeamreactome version 61
86749view09:25, 11 July 2016ReactomeTeamreactome version 56
83402view11:08, 18 November 2015ReactomeTeamVersion54
81600view13:08, 21 August 2015ReactomeTeamVersion53
77057view08:35, 17 July 2014ReactomeTeamFixed remaining interactions
76762view12:12, 16 July 2014ReactomeTeamFixed remaining interactions
75796view11:33, 10 June 2014ReactomeTeamReactome 48 Update
75147view14:09, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74794view08:53, 30 April 2014ReactomeTeamReactome46
44989view14:35, 6 October 2011MartijnVanIerselOntology Term : 'cell adhesion signaling pathway' added !
42016view21:50, 4 March 2011MaintBotAutomatic update
39819view05:51, 21 January 2011MaintBotNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
ACTN1 ProteinP12814 (Uniprot-TrEMBL)
ACTN1ProteinP12814 (Uniprot-TrEMBL)
ARHGEF6 ProteinQ15052 (Uniprot-TrEMBL)
ARHGEF6ProteinQ15052 (Uniprot-TrEMBL)
Afadin:F-actinComplexR-HSA-433726 (Reactome)
BP230:BP180:Plectin:integrin alpha 6 beta 4:Laminin 332ComplexR-HSA-446010 (Reactome)
BP230R-HSA-447012 (Reactome)
Beta-catenin/gamma cateninR-HSA-418993 (Reactome)
CADM1 ProteinQ9BY67 (Uniprot-TrEMBL)
CADM1ProteinQ9BY67 (Uniprot-TrEMBL)
CADM2 ProteinQ8N3J6 (Uniprot-TrEMBL)
CADM3 ProteinQ8N126 (Uniprot-TrEMBL)
CADM3ProteinQ8N126 (Uniprot-TrEMBL)
CD151 ProteinP48509 (Uniprot-TrEMBL)
CD151:BP230:BP180:Plectin:Integrin alpha 6 beta 4: LamininComplexR-HSA-446066 (Reactome)
CD151ProteinP48509 (Uniprot-TrEMBL)
CDH1(155-882) ProteinP12830 (Uniprot-TrEMBL)
CDH10 ProteinQ9Y6N8 (Uniprot-TrEMBL)
CDH11 ProteinP55287 (Uniprot-TrEMBL)
CDH12 ProteinP55289 (Uniprot-TrEMBL)
CDH13 ProteinP55290 (Uniprot-TrEMBL)
CDH15 ProteinP55291 (Uniprot-TrEMBL)
CDH17 ProteinQ12864 (Uniprot-TrEMBL)
CDH18 ProteinQ13634 (Uniprot-TrEMBL)
CDH2 ProteinP19022 (Uniprot-TrEMBL)
CDH24 ProteinQ86UP0 (Uniprot-TrEMBL)
CDH3 ProteinP22223 (Uniprot-TrEMBL)
CDH4 ProteinP55283 (Uniprot-TrEMBL)
CDH6 ProteinP55285 (Uniprot-TrEMBL)
CDH7 ProteinQ9ULB5 (Uniprot-TrEMBL)
CDH8 ProteinP55286 (Uniprot-TrEMBL)
CDH9 ProteinQ9ULB4 (Uniprot-TrEMBL)
COL17A1(1-1497) ProteinQ9UMD9 (Uniprot-TrEMBL)
COL17A1(1-1497)ProteinQ9UMD9 (Uniprot-TrEMBL)
CRB3 ProteinQ9BUF7 (Uniprot-TrEMBL)
CRB3:PALS1:PATJ complexComplexR-HSA-420663 (Reactome)
CRB3ProteinQ9BUF7 (Uniprot-TrEMBL)
CTNNA1 ProteinP35221 (Uniprot-TrEMBL)
CTNNA1ProteinP35221 (Uniprot-TrEMBL)
CTNND1 ProteinO60716 (Uniprot-TrEMBL)
CTNND1ProteinO60716 (Uniprot-TrEMBL)
Ca2+MetaboliteCHEBI:29108 (ChEBI)
Cadherin trans-homodimerComplexR-HSA-418999 (Reactome)
Cadherin:Catenin complexComplexR-HSA-418976 (Reactome)
Classic CadherinR-HSA-418977 (Reactome)
ClaudinR-HSA-419998 (Reactome)
F-actinR-HSA-201877 (Reactome)
F11R ProteinQ9Y624 (Uniprot-TrEMBL)
F11RProteinQ9Y624 (Uniprot-TrEMBL)
FBLIM1 ProteinQ8WUP2 (Uniprot-TrEMBL)
FBLIM1ProteinQ8WUP2 (Uniprot-TrEMBL)
FERMT2 ProteinQ96AC1 (Uniprot-TrEMBL)
FERMT2ProteinQ96AC1 (Uniprot-TrEMBL)
FLNA ProteinP21333 (Uniprot-TrEMBL)
FLNC ProteinQ14315 (Uniprot-TrEMBL)
FilaminR-HSA-446328 (Reactome)
ILK ProteinQ13418 (Uniprot-TrEMBL)
ILK:Integrin beta-1ComplexR-HSA-446408 (Reactome)
ILKProteinQ13418 (Uniprot-TrEMBL)
INADL ProteinQ8NI35 (Uniprot-TrEMBL)
INADLProteinQ8NI35 (Uniprot-TrEMBL)
ITGA6(24-1130) ProteinP23229 (Uniprot-TrEMBL)
ITGB1 ProteinP05556 (Uniprot-TrEMBL)
ITGB1ProteinP05556 (Uniprot-TrEMBL)
ITGB4 ProteinP16144 (Uniprot-TrEMBL)
Integrin

alpha 6:beta

4:Plectin:BP180:Laminin-322 complex
ComplexR-HSA-445997 (Reactome)
Integrin alpha6:beta4:Plectin:BP180 complexComplexR-HSA-445993 (Reactome)
Integrin alpha

6:beta 4:Plectin

complex
ComplexR-HSA-445996 (Reactome)
Integrin alpha6beta4ComplexR-HSA-215997 (Reactome)
JAM-A:PAR-aPKC complexComplexR-HSA-420006 (Reactome)
JUP ProteinP14923 (Uniprot-TrEMBL)
Keratin 5/14R-HSA-446069 (Reactome)
LAMA3 ProteinQ16787 (Uniprot-TrEMBL)
LAMB3 ProteinQ13751 (Uniprot-TrEMBL)
LAMC2 ProteinQ13753 (Uniprot-TrEMBL)
LIMS1 ProteinP48059 (Uniprot-TrEMBL)
LIMS1ProteinP48059 (Uniprot-TrEMBL)
LIMS2 ProteinQ7Z4I7 (Uniprot-TrEMBL)
Laminin-332ComplexR-HSA-216001 (Reactome)
MIG-2:MIGFILINComplexR-HSA-430295 (Reactome)
MIGFILIN:VASPComplexR-HSA-446308 (Reactome)
MLLT4-2 ProteinP55196-2 (Uniprot-TrEMBL)
MLLT4-2ProteinP55196-2 (Uniprot-TrEMBL)
MPP5 ProteinQ8N3R9 (Uniprot-TrEMBL)
MPP5ProteinQ8N3R9 (Uniprot-TrEMBL)
Migfilin:Filamin A:F-actinComplexR-HSA-430323 (Reactome) Interaction of Filamin with Migfiln mediates the association with the Migfilin with actin filaments (Tu et al., 2002).
Necl-1/Necl-2/Necl-3 homodimerR-HSA-420583 (Reactome)
Necl-1/Necl-2/Necl-3 trans homodimerComplexR-HSA-420594 (Reactome)
Necl-1:Necl-2 trans heterodimerComplexR-HSA-420587 (Reactome)
Necl-1:Nectin-1 trans heterodimerComplexR-HSA-420585 (Reactome)
Necl-1:Nectin-3 trans heterodimerComplexR-HSA-420577 (Reactome)
Nectin cis-homodimerComplexR-HSA-433730 (Reactome)
Nectin trans homodimerComplexR-HSA-418972 (Reactome)
Nectin-1 cis homodimerComplexR-HSA-420607 (Reactome)
Nectin-1:Nectin-4 trans heterodimerComplexR-HSA-420609 (Reactome)
Nectin-1:PVRL3 trans heterodimerComplexR-HSA-420601 (Reactome)
Nectin-2 cis homodimerComplexR-HSA-420575 (Reactome)
Nectin-2:PVRL3 transheterodimerComplexR-HSA-420605 (Reactome)
Nectin-3:Necl-2 trans heterodimerComplexR-HSA-420578 (Reactome)
Nectin-4 cis homodimerComplexR-HSA-420606 (Reactome)
Nectin:afadin complexComplexR-HSA-419013 (Reactome)
NectinR-HSA-419017 (Reactome)
PARD3 ProteinQ8TEW0 (Uniprot-TrEMBL)
PARD6A ProteinQ9NPB6 (Uniprot-TrEMBL)
PARD6B ProteinQ9BYG5 (Uniprot-TrEMBL)
PARD6G ProteinQ9BYG4 (Uniprot-TrEMBL)
PARVA ProteinQ9NVD7 (Uniprot-TrEMBL)
PARVA:PaxillinComplexR-HSA-446326 (Reactome)
PARVA:TESK1ComplexR-HSA-446404 (Reactome)
PARVAProteinQ9NVD7 (Uniprot-TrEMBL)
PARVB ProteinQ9HBI1 (Uniprot-TrEMBL)
PARVB:alpha actininComplexR-HSA-446335 (Reactome)
PARVBProteinQ9HBI1 (Uniprot-TrEMBL)
PINCH-ILK-parvin complexComplexR-HSA-432932 (Reactome)
PINCHR-HSA-446104 (Reactome)
PLEC ProteinQ15149 (Uniprot-TrEMBL)
PLECProteinQ15149 (Uniprot-TrEMBL)
PRKCI ProteinP41743 (Uniprot-TrEMBL)
PRV:PVRL3 trans heterodimerComplexR-HSA-420579 (Reactome)
PVR ProteinP15151 (Uniprot-TrEMBL)
PVRL1 ProteinQ15223 (Uniprot-TrEMBL)
PVRL1ProteinQ15223 (Uniprot-TrEMBL)
PVRL2 ProteinQ92692 (Uniprot-TrEMBL)
PVRL3 ProteinQ9NQS3 (Uniprot-TrEMBL)
PVRL3 dimerComplexR-HSA-420590 (Reactome)
PVRL3ProteinQ9NQS3 (Uniprot-TrEMBL)
PVRL4 ProteinQ96NY8 (Uniprot-TrEMBL)
PVRProteinP15151 (Uniprot-TrEMBL)
PXN ProteinP49023 (Uniprot-TrEMBL)
PXNProteinP49023 (Uniprot-TrEMBL)
Par3:Par6:aPKC complexComplexR-HSA-419976 (Reactome)
ParvB/Affixin:Alpha-PixComplexR-HSA-446035 (Reactome)
RSU1 ProteinQ15404 (Uniprot-TrEMBL)
RSU1ProteinQ15404 (Uniprot-TrEMBL)
Rsu-1:Pinch1 complexComplexR-HSA-446302 (Reactome)
TESK1 ProteinQ15569 (Uniprot-TrEMBL)
TESK1ProteinQ15569 (Uniprot-TrEMBL)
Type II hemidesmosomeComplexR-HSA-446086 (Reactome)
VASP ProteinP50552 (Uniprot-TrEMBL)
VASPProteinP50552 (Uniprot-TrEMBL)
VE-cadherin ProteinP33151 (Uniprot-TrEMBL)
alpha/beta parvinR-HSA-446032 (Reactome)
claudin trans-homodimerComplexR-HSA-421252 (Reactome)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
ACTN1R-HSA-430308 (Reactome)
ARHGEF6R-HSA-432946 (Reactome)
Afadin:F-actinArrowR-HSA-433725 (Reactome)
BP230:BP180:Plectin:integrin alpha 6 beta 4:Laminin 332ArrowR-HSA-432956 (Reactome)
BP230:BP180:Plectin:integrin alpha 6 beta 4:Laminin 332R-HSA-446083 (Reactome)
BP230R-HSA-432956 (Reactome)
Beta-catenin/gamma cateninR-HSA-419002 (Reactome)
CADM1R-HSA-420586 (Reactome)
CADM1R-HSA-420595 (Reactome)
CADM3R-HSA-420582 (Reactome)
CADM3R-HSA-420584 (Reactome)
CADM3R-HSA-420586 (Reactome)
CD151:BP230:BP180:Plectin:Integrin alpha 6 beta 4: LamininArrowR-HSA-446083 (Reactome)
CD151:BP230:BP180:Plectin:Integrin alpha 6 beta 4: LamininR-HSA-446077 (Reactome)
CD151R-HSA-446083 (Reactome)
COL17A1(1-1497)R-HSA-432952 (Reactome)
CRB3:PALS1:PATJ complexArrowR-HSA-420661 (Reactome)
CRB3R-HSA-420661 (Reactome)
CTNNA1R-HSA-419002 (Reactome)
CTNND1R-HSA-419002 (Reactome)
Ca2+R-HSA-419001 (Reactome)
Cadherin trans-homodimerArrowR-HSA-419001 (Reactome)
Cadherin:Catenin complexArrowR-HSA-419002 (Reactome)
Classic CadherinR-HSA-419001 (Reactome)
Classic CadherinR-HSA-419002 (Reactome)
ClaudinR-HSA-420019 (Reactome)
F-actinR-HSA-430347 (Reactome)
F-actinR-HSA-433725 (Reactome)
F11RR-HSA-419981 (Reactome)
FBLIM1R-HSA-430341 (Reactome)
FBLIM1R-HSA-430347 (Reactome)
FBLIM1R-HSA-446364 (Reactome)
FERMT2R-HSA-430341 (Reactome)
FilaminR-HSA-430347 (Reactome)
ILK:Integrin beta-1ArrowR-HSA-432897 (Reactome)
ILKR-HSA-432897 (Reactome)
ILKR-HSA-446391 (Reactome)
INADLR-HSA-420661 (Reactome)
ITGB1R-HSA-432897 (Reactome)
Integrin

alpha 6:beta

4:Plectin:BP180:Laminin-322 complex
ArrowR-HSA-446089 (Reactome)
Integrin

alpha 6:beta

4:Plectin:BP180:Laminin-322 complex
R-HSA-432956 (Reactome)
Integrin alpha6:beta4:Plectin:BP180 complexArrowR-HSA-432952 (Reactome)
Integrin alpha6:beta4:Plectin:BP180 complexR-HSA-446089 (Reactome)
Integrin alpha

6:beta 4:Plectin

complex
ArrowR-HSA-432909 (Reactome)
Integrin alpha

6:beta 4:Plectin

complex
R-HSA-432952 (Reactome)
Integrin alpha6beta4R-HSA-432909 (Reactome)
JAM-A:PAR-aPKC complexArrowR-HSA-419981 (Reactome)
Keratin 5/14R-HSA-446077 (Reactome)
LIMS1R-HSA-430311 (Reactome)
Laminin-332R-HSA-446089 (Reactome)
MIG-2:MIGFILINArrowR-HSA-430341 (Reactome)
MIGFILIN:VASPArrowR-HSA-446364 (Reactome)
MLLT4-2R-HSA-419003 (Reactome)
MLLT4-2R-HSA-433725 (Reactome)
MPP5R-HSA-420661 (Reactome)
Migfilin:Filamin A:F-actinArrowR-HSA-430347 (Reactome)
Necl-1/Necl-2/Necl-3 homodimerR-HSA-420592 (Reactome)
Necl-1/Necl-2/Necl-3 trans homodimerArrowR-HSA-420592 (Reactome)
Necl-1:Necl-2 trans heterodimerArrowR-HSA-420586 (Reactome)
Necl-1:Nectin-1 trans heterodimerArrowR-HSA-420582 (Reactome)
Necl-1:Nectin-3 trans heterodimerArrowR-HSA-420584 (Reactome)
Nectin cis-homodimerArrowR-HSA-433711 (Reactome)
Nectin cis-homodimerR-HSA-419011 (Reactome)
Nectin trans homodimerArrowR-HSA-419011 (Reactome)
Nectin-1 cis homodimerR-HSA-420580 (Reactome)
Nectin-1 cis homodimerR-HSA-420598 (Reactome)
Nectin-1:Nectin-4 trans heterodimerArrowR-HSA-420598 (Reactome)
Nectin-1:PVRL3 trans heterodimerArrowR-HSA-420580 (Reactome)
Nectin-2 cis homodimerR-HSA-420591 (Reactome)
Nectin-2:PVRL3 transheterodimerArrowR-HSA-420591 (Reactome)
Nectin-3:Necl-2 trans heterodimerArrowR-HSA-420595 (Reactome)
Nectin-4 cis homodimerR-HSA-420598 (Reactome)
Nectin:afadin complexArrowR-HSA-419003 (Reactome)
NectinR-HSA-419003 (Reactome)
NectinR-HSA-433711 (Reactome)
PARVA:PaxillinArrowR-HSA-446322 (Reactome)
PARVA:TESK1ArrowR-HSA-446372 (Reactome)
PARVAR-HSA-446322 (Reactome)
PARVAR-HSA-446372 (Reactome)
PARVB:alpha actininArrowR-HSA-430308 (Reactome)
PARVBR-HSA-430308 (Reactome)
PARVBR-HSA-432946 (Reactome)
PINCH-ILK-parvin complexArrowR-HSA-446391 (Reactome)
PINCHR-HSA-446391 (Reactome)
PLECR-HSA-432909 (Reactome)
PRV:PVRL3 trans heterodimerArrowR-HSA-420593 (Reactome)
PVRL1R-HSA-420582 (Reactome)
PVRL3 dimerR-HSA-420580 (Reactome)
PVRL3 dimerR-HSA-420591 (Reactome)
PVRL3R-HSA-420584 (Reactome)
PVRL3R-HSA-420593 (Reactome)
PVRL3R-HSA-420595 (Reactome)
PVRR-HSA-420593 (Reactome)
PXNR-HSA-446322 (Reactome)
Par3:Par6:aPKC complexR-HSA-419981 (Reactome)
ParvB/Affixin:Alpha-PixArrowR-HSA-432946 (Reactome)
R-HSA-419001 (Reactome) Cadherins are the major cell adhesion molecules at adherens junctions (AJs). Classical cadherins are Ca2+-dependent, homophilic adhesion molecules that link adjacent cells (Gumbiner, 2005; Halbleib and Nelson, 2006; Pokutta and Weis, 2007). The extracellular domain of classical cadherins consists of five cadherin-type repeats (called "extracellular cadherin" (EC) -domains). In the presence of Ca2+, the monomers form parallel cis-dimers resulting in a rod-like structure (Gumbiner, 2005). The cis-dimers undergo trans homophilic interactions to mediate homotypic cell-cell interactions. The cytoplasmic tails of classical cadherins interact with different proteins (primarily catenins) to regulate cell surface expression levels, linkage to the actin cytoskeleton, and cell signaling. Non-classical cadherins (Atypical cadherins, Proto-cadherins, cadherin-related proteins) have a variable number of cadherin-type repeats, do not associate with catenins, and are not associated with AJs (Halbleib and Nelson, 2006).
R-HSA-419002 (Reactome) The cytoplasmic tails of classical cadherins form a multiprotein complex with alpha-catenin, beta/gamma-catenins and p120 catenin (p120ctn) (Gumbiner, 2005). Beta-catenin and p120ctn directly interact with the cadherin molecule through highly conserved regions in the membrane-distal and membrane-proximal domains, respectively, of the cadherin. The interactions with beta-catenin and p120ctn regulate cadherin localization at cell-cell contacts as well as its adhesive activity (Halbleib and Nelson, 2006). The association of beta-catenin and alpha-catenin probably serves to link the cadherin-catenin complex to the F-actin cytoskeleton through the protein ELPIN (Abe and Takeichi, 2008). Independently of its association with the cadherin-catenin complex, alpha-catenin also regulates the bundling and growth of actin filaments at sites of cell-cell contact formation (Drees et al., 2005; Weis and Nelson, 2006).
R-HSA-419003 (Reactome) Nectins are immunoglobulin-like cell adhesion molecules comprising a family of four members, nectin 1 - 4 (Takai and Nakanishi, 2003). In contrast to classical cadherins which interact only homophilically, nectins undergo trans-homophilic and trans-heterophilic interactions with nectins and nectin-like molecules (Takai et al., 2008b). Nectins cooperate with cadherins in regulating the formation of adherens junctions (AJs) and the strength of cell-cell adhesion. Nectins are linked to the underlying actin cytoskeleton through their interaction with the actin-binding protein Afadin (Takai et al., 2008a). Nectin-based cell–cell adhesions contribute to formation of many types of cell-cell junctions including AJs, tight junctions, and synaptic junctions.
R-HSA-419011 (Reactome) Nectins are Ca(2+)-independent cell adhesion molecules which interact homophilically and heterophilically in trans to form cell-cell adhesions (reviewed in (Sakisaka et al., 2007; Takai et al., 2008). Each nectin first forms homo-cis-dimers and then homo- or hetero-trans-dimers through the extracellular region, causing cell–cell adhesion. The Nectin protein family is made up of four members, nectin-1, -2, -3, and -4, all of which have an extracellular region with three Ig-like loops, a single transmembrane region, and a cytoplasmic tail region.
R-HSA-419981 (Reactome) PAR-3 exists in a ternary complex with aPKC and PAR-6 to form the PAR-aPKC complex (Macara, 2004; Suzuki and Ohno, 2006). This complex is critically involved in the development of Tight Junctions (TJs) from primordial spot-like Adherens Junctions (AJs) (Suzuki et al., 2002). PAR-3 directly interacts with Junctional Adhesion Molecules (JAM)-A, -B, and -C (Ebnet et al., 2001; Ebnet et al., 2004).The interaction with JAM-A might anchor the PAR-aPKC complex to TJs but might also be necessary to recruit the PAR-aPKC complex to primordial spot-like AJs where it becomes activated in response to cell-cell adhesion (reviewed in (Ebnet et al., 2008). The PAR-aPKC complex might also be physically linked to the second polarity protein complex at TJs, the CRB3-Pals1-PATJ complex through a direct interaction between PAR-6 and Pals1 (Hurd et al., 2003).
R-HSA-420019 (Reactome) Claudins are the major cell adhesion molecules in tight junctions and are involved in regulating the paracellular flux of water-soluble molecules between adjacent cells (reviewed in (Furuse and Tsukita, 2006). Claudins create paired strands through homophilic and heterophilic cis and trans interactions. A strand of one cell associates laterally with a strand in the apposing membrane of an adjacent cell creating a paired TJ strand (Tsukita et al., 2001). The TJ strands contain aqueous pores with size and charge selectivity that are permeable to water-soluble molecules. Differences in the barrier properties in epithelia of different tissues have been explained by the expression of a unique set of claudins in a given tissue (Van Itallie and Anderson, 2006). 24 claudins were identified in humans, which allows a large number of possible combinations and specific barrier properties.
R-HSA-420580 (Reactome) Nectin-1 and Nectin 3 interact forming a trans heterodimer.
R-HSA-420582 (Reactome) Necl-1 displays Ca2+-independent heterophilic cell-cell adhesion activity with Nectin-1 (Kakunaga et al., 2005).
R-HSA-420584 (Reactome) Necl-1 displays Ca2+-independent heterophilic cell-cell adhesion activity with Nectin-3 (Kakunaga et al., 2005).
R-HSA-420586 (Reactome) Necl-1 displays Ca2+-independent heterophilic cell-cell adhesion activity with Necl-2 (Kakunaga et al., 2005).
R-HSA-420591 (Reactome) Nectin-2 and Nectin-3 interact forming a trans heterodimer.
R-HSA-420592 (Reactome) The nectin-like (Necl) family comprises five members, called Necl-1 to -5. Necl have an overall organization like that of nectins with three Ig-like domains, a transmembrane region and a cytoplasmic domain. Necls have a greater variety of functions than nectins and are ubiquitously expressed. In contrast to nectins, Necls do not interact with afadin. Transhomodimerization has been described for Necl-1, -2 and -3 but not for Necl-4 and -5. (Sakisaka et al., 2007; Sakisaka and Takai, 2004; Takai et al., 2008).
R-HSA-420593 (Reactome) Necl-5/PVR and Nectin-3/PVRL3 interact forming a trans heterodimer.
R-HSA-420595 (Reactome) Necl-2 and Nectin 3 form a trans heterodimer.
R-HSA-420598 (Reactome) Nectin-1 and Nectin-4 interact forming a trans heterodimer.
R-HSA-420661 (Reactome) The CRB3–Pals1–PATJ complex is the second major cell polarity protein complex at Tight Junctions (TJs) (Shin et al., 2006). The integral membrane protein CRB3 localizes to the apical domain of epithelial cells and is concentrated at TJs. CRB3 directly associates with Pals1 which interacts with PATJ, a proteins consisting of 10 PDZ domains. The interaction with CRB3 might recruit the Pals1-PATJ complex to TJs (Lemmers et al., 2002; Roh et al., 2003). Although its precise functions of the individual components have not been established, the complex is required for TJ formation, in part through the stabilization of apical and lateral components of tight junctions (Michel et al., 2005; Shin et al., 2005).
R-HSA-430308 (Reactome) PARVB interacts with the actin cross-linking protein Alpha-actinin (Yamaji et al. 2004). The ILK-PARVB complex may serve as an integrin-anchoring site for alpha-actinin and thereby mediate integrin signaling to alpha-actinin, which has been shown to play an important role in actin polymerization at focal adhesions (Yamaji et al., 2004).
R-HSA-430311 (Reactome) The Ras suppressor, Rsu-1, interacts with the LIM 5 domain of PINCH1 (but not PINCH2) and may inhibit cell migration by stabilizing the Pinch-ILK-parvin adhesion complex (Dougherty et al., 2008; Kadrmas et al., 2004).
R-HSA-430341 (Reactome) Migfilin functions in cell shape modulation regulating filamin-mediated cross-linking and stabilization of actin filaments. Migfilin is recruited to cell–Extra Cellular Matrix adhesion sites in a variety of fibroblasts, epithelial, and endothelial cells by interaction with Mig-2 (Tu et al., 2003).
R-HSA-430347 (Reactome) Migfilin associates with actin filaments as a result of its interaction with filamin (Tu et al., 2003). Migfilin associates with actin filaments and loss of migfilin decreases the level of F-actin suggesting that, in addition to providing an anchoring site for actin filaments at cell-ECM adhesions, migfilin also functions in the regulation of filamin-mediated cross-linking and stabilization of actin filaments (Tu et al., 2003).
R-HSA-432897 (Reactome) ILK interacts with the cytoplasmic domain of beta1-integrin (Hannigan et al., 1996).
R-HSA-432909 (Reactome) The actin-binding domain of plectin interacts with the first pair of FNIII repeats and the N-terminal 35 amino acids of the connecting segment of integrin b4 ( Geerts et al., 1999; Niessen et al., 1997; Koster et al., 2004). This interaction is thought to be the initial step in hemidesmosome (HD) assembly and is critical for the mechanical stability of the HD. This interaction is destabilized when HD disassembly is required, for example, to allow cell migration during wound healing. The Integrin a6b4 also associates extracellularly with laminin-332 (See Koster et al., 2003).
R-HSA-432946 (Reactome) The Rho GTPases, Cdc42 and Rac1, play critical roles in cell migration by integrating cell-substrate adhesion and actin polymerization. PARVB/affixin appears to participate in the activation of Rac and Cdc42 by associating with alpha PIX through its CH1 domain (Mishima et al., 2004; Rosenberger et al., 2005). This activity of PARVB/affixin could promote the polymerization of actin through the activation of downstream effectors of Rac1/Cdc42, including WASP-Arp2/3 and Mena/VASP. Alpha-PIX, ILK and PARVB can be found at the leading edge of spreading cells (Rosenberger et al., 2005 ), and it is likely that activation of Rac1 and Cdc42 at the lamellipodia in some cells is stimulated by interactions of aPIX with PARVB and regulated by interaction of ILK and PARVB (see Sepulveda and Wu, 2005 ).
R-HSA-432952 (Reactome) BP180 interacts with Plectin following the association of Plectin with Integrin b4 (b4) (Koster et al., 2003). It is not clear whether the binding of BP180 to Plectin and b4 occurs sequentially or at the same time as the interaction between BP180 and Laminin?332.
R-HSA-432956 (Reactome) Following the association of BP180 with the forming hemidesmosome, BP230 is recruited through associations with BP180 and a region on beta 4 integrin that includes the C-terminal 21 amino acids of the connecting segment and the second pair of FNIII repeats (Hopkinson et al.,2000).
R-HSA-433711 (Reactome) The Nectin family of Ca2+-independent cell adhesion molecules (CAMs) is comprised of four members, nectin-1, nectin-2, nectin-3, and nectin-4 (reviewed in Sakisaka et al., 2007). Each nectin first forms homophilic cis-dimers and then forms homophilic or heterophilic trans-dimers involved in cell–cell adhesion. Heterophilic trans-interactions are stronger than homophilic trans-interactions.
R-HSA-433725 (Reactome) Afadin serves as a linker of the actin cytoskeleton to the plasma membrane at cell-to-cell Adherens Junctions (Mandai et al., 1997).
R-HSA-446077 (Reactome) BP230 interacts with cytokeratins K5/K14 (Fontao et al., 2003).
R-HSA-446083 (Reactome) CD151 interacts with the extracellular domain of the integrin alpha 6 subunit. CD151 is thought to play a role in the formation and stability of hemidesmosomes by providing a framework for the spatial organization of the hemidesmosomal components (Sterk et al., 2000).
R-HSA-446089 (Reactome) BP180 interacts with Plectin following the association of Plectin with Integrin b4 (b4) (Koster et al., 2003). It is not clear whether the binding of BP180 to Plectin and b4 occurs sequentially or at the same time as the interaction between BP180 and Laminin?332.
R-HSA-446322 (Reactome) The focal adhesion protein alpha-parvin, interacts with paxillin, through the C-terminal CH-containing fragment of the alpha-parvin and paxillin LD motif (Wang et al., 2008; Lorenz et al., 2008). This interaction likely contributes to the localization of the PINCH-ILK-parvin complexes to focal adhesions.
R-HSA-446364 (Reactome) Migfilin interacts with VASP and regulates VASP localization to cell-matrix adhesions (Zhang et al., 2006). Interaction between migfilin and VASP is critical for migfilin-mediated regulation of cell migration (Zhang et al., 2006).
R-HSA-446372 (Reactome) The association of PARVA with TESK1 appears to suppress cell spreading (Lalonde et al. 2005). TESK1 can phosphorylate cofilin and promote F-actin polymerization and cell spreading (Tsumura et al., 2005 ; Toshima et al., 2001; Leeksma et al., 2002). PARVA associates with testicular protein kinase 1 (TESK1) and inhibits its activity (Lalonde et al. 2005).
R-HSA-446391 (Reactome) The PINCH-ILK-parvin complex (Tu et al., 2001; Zhang et al., 2002; Li et al., 1999) localizes to focal adhesions and plays a critical role in the regulation of cell adhesion, cell shape modulation, motility and ECM deposition (Velyvis et al., 2001; Braun et al, 2003). ILK binds PINCH through its N-terminal domain and binds PARVA or PARVB through its C-terminal domain, resulting in formation of the ternary PINCH-ILK-parvin complex (Tu et al., 2001). These complexes form before they are localized to integrin-rich adhesion sites (Zhang et al., 2002). Formation of the ILK-PINCH-parvin complexes stabilizes these proteins by protecting them from degradation by the proteasome (Fukuda et al., 2003).
RSU1R-HSA-430311 (Reactome)
Rsu-1:Pinch1 complexArrowR-HSA-430311 (Reactome)
TESK1R-HSA-446372 (Reactome)
Type II hemidesmosomeArrowR-HSA-446077 (Reactome)
VASPR-HSA-446364 (Reactome)
alpha/beta parvinR-HSA-446391 (Reactome)
claudin trans-homodimerArrowR-HSA-420019 (Reactome)
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