Cell junction organization (Homo sapiens)

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1525251520151422, 291012, 2317194, 62302118273, 8, 2811, 267102715616, 2411513945AfadinF-actin Par3Par6aPKC complex Integrin alpha 6beta 4PlectinBP180Laminin-322 complex Nectin trans homodimer Nectin-3Necl-2 trans heterodimer BP230BP180Plectinintegrin alpha 6 beta 4Laminin 332 Integrin alpha6beta4 cytosolLaminin-332 CD151BP230BP180PlectinIntegrin alpha 6 beta 4 Laminin ILKIntegrin beta-1 Integrin alpha 6beta 4Plectin complex Integrin alpha 6beta 4Plectin complex Integrin alpha 6beta 4Plectin complex PINCH-ILK-parvin complex Integrin alpha6beta4PlectinBP180 complex Nectin-2 cis homodimer PAR-6 Integrin alpha 6beta 4Plectin complex PVRL3 dimer Classic Cadherin Integrin alpha6beta4 Necl-1/Necl-2/Necl-3 trans homodimer ParvB/AffixinAlpha-Pix Necl-1Necl-2 trans heterodimer Laminin-332 Necl-1/Necl-2/Necl-3 homodimer Laminin-332 Rsu-1Pinch1 complex Type II hemidesmosome MIG-2MIGFILIN PINCH Laminin-332 Integrin alpha 6beta 4PlectinBP180Laminin-322 complex Necl-1Nectin-1 trans heterodimer Nectin Integrin alpha6beta4 Necl-2 dimer CRB3PALS1PATJ complex CadherinCatenin complex Nectin cis-homodimer PVRL3 dimer Cadherin trans-homodimer Nectin-1Nectin-4 trans heterodimer Nectin-4 cis homodimer PVRL3 dimer Par3Par6aPKC complex Nectin-1PVRL3 trans heterodimer Integrin alpha 6beta 4Plectin complex Nectin Nectinafadin complex CD151BP230BP180PlectinIntegrin alpha 6 beta 4 Laminin Nectin cis-homodimer cytosolClassic Cadherin MIGFILINVASP PARVAPaxillin PARVBalpha actinin Integrin alpha 6beta 4PlectinBP180Laminin-322 complex Integrin alpha 6beta 4PlectinBP180Laminin-322 complex Necl-1Nectin-3 trans heterodimer BP230BP180Plectinintegrin alpha 6 beta 4Laminin 332 Laminin-332 Necl-3 dimer Filamin Nectin-2PVRL3 transheterodimer MigfilinFilamin AF-actin Integrin alpha6beta4 Beta-catenin/gamma catenin Integrin alpha6beta4 Nectin-2 cis homodimer Necl-1 dimer claudin trans-homodimer Nectin-1 cis homodimer PRVPVRL3 trans heterodimer PAR-6 PARVATESK1 Integrin alpha6beta4 Nectin-1 cis homodimer Integrin alpha6beta4 Nectin Nectin-1 cis homodimer JAM-APAR-aPKC complex BP230BP180Plectinintegrin alpha 6 beta 4Laminin 332 Nectin-4 cis homodimer Integrin alpha 6beta 4Plectin complex Nectin-1 cis homodimerCADM3 PLEC RSU1 CDH12 claudin trans-homodimerITGB1 PVRL1 CDH13 FBLIM1 CD151BP230BP180PlectinIntegrin alpha 6 beta 4 LamininNectin-2 cis homodimerPARVAPaxillinITGA6CRB3 Nectinafadin complexFERMT2FLNA PVRL1 PVRL3 Cadherin trans-homodimerPARVATESK1PVRL4 Integrin alpha6beta4PLEC CDH10 CADM3 CDH6 CD151PINCHMigfilinFilamin AF-actinLAMC2 JUP CTNNA1PLEC CDH7 F-actinILK FBLIM1Integrin alpha6beta4PlectinBP180 complexNectin-4 cis homodimerCOL17A1Nectin-1Nectin-4 trans heterodimerCDH11 PVRL3 ITGA6FBLIM1 TESK1 LIMS1 CDH10 MIG-2MIGFILINCDH7 ITGB4 CADM3 Ca2+PLEC Laminin-332CD151 CDH24 LIMS2 FERMT2 Necl-1Necl-2 trans heterodimerJAM-APAR-aPKC complexMLLT4-2PVRL2 F11RACTN1PLEC MIGFILINVASPAfadinF-actinCTNND1 ARHGEF6 CDH5 CDH6 CDH24 FBLIM1 Keratin 5/14CADM3 LAMB3 Nectin cis-homodimerLAMC2 ITGB4 ILK PARVA TESK1PVRL4 Necl-1Nectin-1 trans heterodimerVASP LAMA3 CADM3CDH8 ILKIntegrin beta-1Par3Par6aPKC complexNectin trans homodimerCOL17A1INADLLIMS1PVRL3 PVRL3 ITGA6PARD6A PVRL2 Type II hemidesmosomeCADM1 Nectin-2PVRL3 transheterodimerPINCH-ILK-parvin complexITGB4 MPP5 PARD6G CDH13 PARVBalpha actininPVRL1 PVRL4 CADM1 COL17A1Nectin-1PVRL3 trans heterodimerPVRITGA6CadherinCatenin complexPVRL4 LAMA3 Beta-catenin/gamma cateninCDH3 CADM2 CTNND1PVRL3CDH2 FilaminPARVAFLNC ClaudinBP230BP180Plectinintegrin alpha 6 beta 4Laminin 332CDH15 PVRL2 MLLT4-2 PLECLAMB3 CDH9 PVRL1 PARD3 LAMB3 PARD6B Classic CadherinCOL17A1CADM1CADM1 PVR PVRL1 PARVBPVRL3 CDH8 Nectin-3Necl-2 trans heterodimerPVRL3 LAMB3 MLLT4-2 Rsu-1Pinch1 complexNecl-1Nectin-3 trans heterodimerLAMC2 PRKCIPLEC ARHGEF6CDH5 ITGB4 Necl-1/Necl-2/Necl-3 homodimerLAMC2 PVRL3 dimerLAMA3 CTNNA1 MPP5PXN VASPNectinCDH12 CRB3PALS1PATJ complexCDH1PVRL1CDH1PARD6B PARVA LAMC2 LAMA3 ITGB4 Integrin alpha 6beta 4PlectinBP180Laminin-322 complexCOL17A1PARD6G F11R ITGA6PARVB CDH3 PVRL1 CRB3CD151 CDH18 alpha/beta parvinLIMS1 ITGB4 PARD6A COL17A1PARD3 PVRL4 LAMA3 ITGA6PARVB PRKCIITGB1CDH4 PVRL2 RSU1CDH18 ITGB4 PVRL1 PVRL3 ACTN1 INADL PRVPVRL3 trans heterodimerCDH11 CDH9 Necl-1/Necl-2/Necl-3 trans homodimerPVRL2 CDH4 PVRL3 ILKPXNPVRL3 Integrin alpha 6beta 4Plectin complexCDH15 ITGA6BP230LAMB3 CDH2 ParvB/AffixinAlpha-Pix


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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-actinComplexREACT_19820 (Reactome)
BP230

BP180 Plectin integrin alpha 6 beta 4

Laminin 332
ComplexREACT_20979 (Reactome)
BP230ProteinREACT_25566 (Reactome)
Beta-catenin/gamma cateninProteinREACT_19976 (Reactome)
CADM1 ProteinQ9BY67 (Uniprot-TrEMBL)
CADM1ProteinQ9BY67 (Uniprot-TrEMBL)
CADM2 ProteinQ8N3J6 (Uniprot-TrEMBL)
CADM3 ProteinQ8N126 (Uniprot-TrEMBL)
CADM3ProteinQ8N126 (Uniprot-TrEMBL)
CD151

BP230 BP180 Plectin Integrin alpha 6 beta 4

Laminin
ComplexREACT_21118 (Reactome)
CD151 ProteinP48509 (Uniprot-TrEMBL)
CD151ProteinP48509 (Uniprot-TrEMBL)
CDH10 ProteinQ9Y6N8 (Uniprot-TrEMBL)
CDH11 ProteinP55287 (Uniprot-TrEMBL)
CDH12 ProteinP55289 (Uniprot-TrEMBL)
CDH13 ProteinP55290 (Uniprot-TrEMBL)
CDH15 ProteinP55291 (Uniprot-TrEMBL)
CDH18 ProteinQ13634 (Uniprot-TrEMBL)
CDH1ProteinP12830 (Uniprot-TrEMBL)
CDH2 ProteinP19022 (Uniprot-TrEMBL)
CDH24 ProteinQ86UP0 (Uniprot-TrEMBL)
CDH3 ProteinP22223 (Uniprot-TrEMBL)
CDH4 ProteinP55283 (Uniprot-TrEMBL)
CDH5 ProteinP33151 (Uniprot-TrEMBL)
CDH6 ProteinP55285 (Uniprot-TrEMBL)
CDH7 ProteinQ9ULB5 (Uniprot-TrEMBL)
CDH8 ProteinP55286 (Uniprot-TrEMBL)
CDH9 ProteinQ9ULB4 (Uniprot-TrEMBL)
COL17A1ProteinQ9UMD9 (Uniprot-TrEMBL)
CRB3

PALS1

PATJ complex
ComplexREACT_20032 (Reactome)
CRB3 ProteinQ9BUF7 (Uniprot-TrEMBL)
CRB3ProteinQ9BUF7 (Uniprot-TrEMBL)
CTNNA1 ProteinP35221 (Uniprot-TrEMBL)
CTNNA1ProteinP35221 (Uniprot-TrEMBL)
CTNND1 ProteinO60716 (Uniprot-TrEMBL)
CTNND1ProteinO60716 (Uniprot-TrEMBL)
Ca2+MetaboliteCHEBI:29108 (ChEBI)
Cadherin Catenin complexComplexREACT_20065 (Reactome)
Cadherin trans-homodimerComplexREACT_19942 (Reactome)
Classic CadherinProteinREACT_20296 (Reactome)
ClaudinProteinREACT_20372 (Reactome)
F-actinREACT_20433 (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)
FilaminProteinREACT_20988 (Reactome)
ILK Integrin beta-1ComplexREACT_20766 (Reactome)
ILK ProteinQ13418 (Uniprot-TrEMBL)
ILKProteinQ13418 (Uniprot-TrEMBL)
INADL ProteinQ8NI35 (Uniprot-TrEMBL)
INADLProteinQ8NI35 (Uniprot-TrEMBL)
ITGA6ProteinP23229 (Uniprot-TrEMBL)
ITGB1 ProteinP05556 (Uniprot-TrEMBL)
ITGB1ProteinP05556 (Uniprot-TrEMBL)
ITGB4 ProteinP16144 (Uniprot-TrEMBL)
Integrin alpha 6

beta 4 Plectin BP180

Laminin-322 complex
ComplexREACT_20915 (Reactome)
Integrin alpha 6

beta 4

Plectin complex
ComplexREACT_21067 (Reactome)
Integrin alpha6

beta4 Plectin

BP180 complex
ComplexREACT_21046 (Reactome)
Integrin alpha6beta4ComplexREACT_14337 (Reactome)
JAM-A PAR-aPKC complexComplexREACT_20246 (Reactome)
JUP ProteinP14923 (Uniprot-TrEMBL)
Keratin 5/14REACT_20869 (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-332ComplexREACT_14602 (Reactome)
MIG-2 MIGFILINComplexREACT_21097 (Reactome)
MIGFILIN VASPComplexREACT_21228 (Reactome)
MLLT4-2 ProteinP55196-2 (Uniprot-TrEMBL)
MLLT4-2ProteinP55196-2 (Uniprot-TrEMBL)
MPP5 ProteinQ8N3R9 (Uniprot-TrEMBL)
MPP5ProteinQ8N3R9 (Uniprot-TrEMBL)
Migfilin

Filamin A

F-actin
ComplexREACT_20733 (Reactome) Interaction of Filamin with Migfiln mediates the association with the Migfilin with actin filaments (Tu et al., 2002).
Necl-1 Necl-2 trans heterodimerComplexREACT_20182 (Reactome)
Necl-1 Nectin-1 trans heterodimerComplexREACT_19689 (Reactome)
Necl-1 Nectin-3 trans heterodimerComplexREACT_19782 (Reactome)
Necl-1/Necl-2/Necl-3 homodimerComplexREACT_19578 (Reactome)
Necl-1/Necl-2/Necl-3 trans homodimerComplexREACT_19789 (Reactome)
Nectin afadin complexComplexREACT_20350 (Reactome)
Nectin cis-homodimerComplexREACT_19521 (Reactome)
Nectin trans homodimerComplexREACT_19779 (Reactome)
Nectin-1 Nectin-4 trans heterodimerComplexREACT_20421 (Reactome)
Nectin-1 PVRL3 trans heterodimerComplexREACT_20025 (Reactome)
Nectin-1 cis homodimerComplexREACT_19460 (Reactome)
Nectin-2 PVRL3 transheterodimerComplexREACT_20370 (Reactome)
Nectin-2 cis homodimerComplexREACT_20053 (Reactome)
Nectin-3 Necl-2 trans heterodimerComplexREACT_19977 (Reactome)
Nectin-4 cis homodimerComplexREACT_20206 (Reactome)
NectinProteinREACT_20136 (Reactome)
PARD3 ProteinQ8TEW0 (Uniprot-TrEMBL)
PARD6A ProteinQ9NPB6 (Uniprot-TrEMBL)
PARD6B ProteinQ9BYG5 (Uniprot-TrEMBL)
PARD6G ProteinQ9BYG4 (Uniprot-TrEMBL)
PARVA PaxillinComplexREACT_21170 (Reactome)
PARVA TESK1ComplexREACT_21038 (Reactome)
PARVA ProteinQ9NVD7 (Uniprot-TrEMBL)
PARVAProteinQ9NVD7 (Uniprot-TrEMBL)
PARVB alpha actininComplexREACT_21104 (Reactome)
PARVB ProteinQ9HBI1 (Uniprot-TrEMBL)
PARVBProteinQ9HBI1 (Uniprot-TrEMBL)
PINCH-ILK-parvin complexComplexREACT_20853 (Reactome)
PINCHProteinREACT_20717 (Reactome)
PLEC ProteinQ15149 (Uniprot-TrEMBL)
PLECProteinQ15149 (Uniprot-TrEMBL)
PRKCIProteinP41743 (Uniprot-TrEMBL)
PRV PVRL3 trans heterodimerComplexREACT_19715 (Reactome)
PVR ProteinP15151 (Uniprot-TrEMBL)
PVRL1 ProteinQ15223 (Uniprot-TrEMBL)
PVRL1ProteinQ15223 (Uniprot-TrEMBL)
PVRL2 ProteinQ92692 (Uniprot-TrEMBL)
PVRL3 ProteinQ9NQS3 (Uniprot-TrEMBL)
PVRL3 dimerComplexREACT_19940 (Reactome)
PVRL3ProteinQ9NQS3 (Uniprot-TrEMBL)
PVRL4 ProteinQ96NY8 (Uniprot-TrEMBL)
PVRProteinP15151 (Uniprot-TrEMBL)
PXN ProteinP49023 (Uniprot-TrEMBL)
PXNProteinP49023 (Uniprot-TrEMBL)
Par3

Par6

aPKC complex
ComplexREACT_19423 (Reactome)
ParvB/Affixin Alpha-PixComplexREACT_20814 (Reactome)
RSU1 ProteinQ15404 (Uniprot-TrEMBL)
RSU1ProteinQ15404 (Uniprot-TrEMBL)
Rsu-1 Pinch1 complexComplexREACT_20937 (Reactome)
TESK1 ProteinQ15569 (Uniprot-TrEMBL)
TESK1ProteinQ15569 (Uniprot-TrEMBL)
Type II hemidesmosomeComplexREACT_20848 (Reactome)
VASP ProteinP50552 (Uniprot-TrEMBL)
VASPProteinP50552 (Uniprot-TrEMBL)
alpha/beta parvinProteinREACT_20989 (Reactome)
claudin trans-homodimerComplexREACT_20391 (Reactome)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
ACTN1REACT_20671 (Reactome)
ARHGEF6REACT_20672 (Reactome)
BP230

BP180 Plectin integrin alpha 6 beta 4

Laminin 332
REACT_20665 (Reactome)
BP230REACT_20561 (Reactome)
Beta-catenin/gamma cateninREACT_19131 (Reactome)
CADM1REACT_19130 (Reactome)
CADM1REACT_19220 (Reactome)
CADM3REACT_19130 (Reactome)
CADM3REACT_19202 (Reactome)
CADM3REACT_19267 (Reactome)
CD151

BP230 BP180 Plectin Integrin alpha 6 beta 4

Laminin
REACT_20615 (Reactome)
CD151REACT_20665 (Reactome)
COL17A1REACT_20589 (Reactome)
CRB3REACT_19144 (Reactome)
CTNNA1REACT_19131 (Reactome)
CTNND1REACT_19131 (Reactome)
Ca2+REACT_19416 (Reactome)
Classic CadherinREACT_19131 (Reactome)
Classic CadherinREACT_19416 (Reactome)
F-actinREACT_19163 (Reactome)
F-actinREACT_20513 (Reactome)
F11RREACT_19353 (Reactome)
FBLIM1REACT_20513 (Reactome)
FBLIM1REACT_20555 (Reactome)
FBLIM1REACT_20572 (Reactome)
FERMT2REACT_20555 (Reactome)
FilaminREACT_20513 (Reactome)
ILKREACT_20645 (Reactome)
ILKREACT_20656 (Reactome)
INADLREACT_19144 (Reactome)
ITGB1REACT_20656 (Reactome)
Integrin alpha 6

beta 4 Plectin BP180

Laminin-322 complex
REACT_20561 (Reactome)
Integrin alpha 6

beta 4

Plectin complex
REACT_20589 (Reactome)
Integrin alpha6

beta4 Plectin

BP180 complex
REACT_20660 (Reactome)
Integrin alpha6beta4REACT_20528 (Reactome)
Keratin 5/14REACT_20615 (Reactome)
LIMS1REACT_20616 (Reactome)
Laminin-332REACT_20660 (Reactome)
MLLT4-2REACT_19163 (Reactome)
MLLT4-2REACT_19214 (Reactome)
MPP5REACT_19144 (Reactome)
Nectin-1 cis homodimerREACT_19201 (Reactome)
Nectin-1 cis homodimerREACT_19302 (Reactome)
Nectin-2 cis homodimerREACT_19176 (Reactome)
Nectin-4 cis homodimerREACT_19201 (Reactome)
NectinREACT_19214 (Reactome)
PARVAREACT_20542 (Reactome)
PARVAREACT_20609 (Reactome)
PARVBREACT_20671 (Reactome)
PARVBREACT_20672 (Reactome)
PINCHREACT_20645 (Reactome)
PLECREACT_20528 (Reactome)
PVRL1REACT_19202 (Reactome)
PVRL3 dimerREACT_19176 (Reactome)
PVRL3 dimerREACT_19302 (Reactome)
PVRL3REACT_19151 (Reactome)
PVRL3REACT_19220 (Reactome)
PVRL3REACT_19267 (Reactome)
PVRREACT_19151 (Reactome)
PXNREACT_20542 (Reactome)
Par3

Par6

aPKC complex
REACT_19353 (Reactome)
REACT_19130 (Reactome) Necl-1 displays Ca2+-independent heterophilic cell-cell adhesion activity with Necl-2 (Kakunaga et al., 2005).
REACT_19131 (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).
REACT_19144 (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).
REACT_19151 (Reactome) Necl-5/PVR and Nectin-3/PVRL3 interact forming a trans heterodimer.
REACT_19163 (Reactome) Afadin serves as a linker of the actin cytoskeleton to the plasma membrane at cell-to-cell Adherens Junctions (Mandai et al., 1997).
REACT_19169 (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.
REACT_19176 (Reactome) Nectin-2 and Nectin-3 interact forming a trans heterodimer.
REACT_19179 (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).
REACT_19201 (Reactome) Nectin-1 and Nectin-4 interact forming a trans heterodimer.
REACT_19202 (Reactome) Necl-1 displays Ca2+-independent heterophilic cell-cell adhesion activity with Nectin-1 (Kakunaga et al., 2005).
REACT_19214 (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.
REACT_19220 (Reactome) Necl-2 and Nectin 3 form a trans heterodimer.
REACT_19267 (Reactome) Necl-1 displays Ca2+-independent heterophilic cell-cell adhesion activity with Nectin-3 (Kakunaga et al., 2005).
REACT_19302 (Reactome) Nectin-1 and Nectin 3 interact forming a trans heterodimer.
REACT_19338 (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.
REACT_19353 (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).
REACT_19364 (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.
REACT_19416 (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).
REACT_20513 (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).
REACT_20528 (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).
REACT_20542 (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.
REACT_20555 (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).
REACT_20561 (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).
REACT_20572 (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).
REACT_20589 (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.
REACT_20609 (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).
REACT_20615 (Reactome) BP230 interacts with cytokeratins K5/K14 (Fontao et al., 2003).
REACT_20616 (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).
REACT_20645 (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).
REACT_20656 (Reactome) ILK interacts with the cytoplasmic domain of beta1-integrin (Hannigan et al., 1996).
REACT_20660 (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.
REACT_20665 (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).
REACT_20671 (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).
REACT_20672 (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 ).
RSU1REACT_20616 (Reactome)
TESK1REACT_20609 (Reactome)
VASPREACT_20572 (Reactome)
alpha/beta parvinREACT_20645 (Reactome)
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