Cell junction organization (Homo sapiens)
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- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Yamagata M, Weiner JA, Sanes JR.; ''Sidekicks: synaptic adhesion molecules that promote lamina-specific connectivity in the retina.''; PubMed Europe PMC Scholia
- 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
- 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
- de Pereda JM, Lillo MP, Sonnenberg A.; ''Structural basis of the interaction between integrin alpha6beta4 and plectin at the hemidesmosomes.''; PubMed Europe PMC Scholia
- 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
- LaLonde DP, Brown MC, Bouverat BP, Turner CE.; ''Actopaxin interacts with TESK1 to regulate cell spreading on fibronectin.''; PubMed Europe PMC Scholia
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Hülsken J, Birchmeier W, Behrens J.; ''E-cadherin and APC compete for the interaction with beta-catenin and the cytoskeleton.''; PubMed Europe PMC Scholia
- 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
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External references
DataNodes
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Name | Type | Database reference | Comment |
---|---|---|---|
Afadin | Protein | P55196-2 (UniProt) | |
Afadin:F-actin | Complex | REACT_19820 (Reactome) | |
Alpha-Pix | Protein | Q15052 (UniProt) | |
Alpha-actinin 1 | Protein | P12814 (UniProt) | |
BP180 | Protein | Q9UMD9 (UniProt) | |
BP230 | Protein | REACT_25566 (Reactome) | |
BP230:BP180:
Plectin:integrin alpha 6 beta 4: Laminin 332 | Complex | REACT_20979 (Reactome) | |
Beta-catenin/gamma
catenin | Protein | REACT_19976 (Reactome) | |
CD151 | Protein | P48509 (UniProt) | |
CD151:BP230:BP180:
Plectin:Integrin alpha 6 beta 4: Laminin | Complex | REACT_21118 (Reactome) | |
CRB3 | Protein | Q9BUF7 (UniProt) | |
CRB3:PALS1:PATJ
complex | Complex | REACT_20032 (Reactome) | |
Cadherin trans-
homodimer | Complex | REACT_19942 (Reactome) | |
Cadherin:Catenin
complex | Complex | REACT_20065 (Reactome) | |
Calcium | Metabolite | 29108 (ChEBI) | |
Classic
Cadherin | Protein | REACT_20296 (Reactome) | |
Claudin | Protein | REACT_20372 (Reactome) | |
F-actin | Unknown | REACT_20433 (Reactome) | |
Filamin | Protein | REACT_20988 (Reactome) | |
ILK | Protein | Q13418 (UniProt) | |
ILK:Integrin beta-1 | Complex | REACT_20766 (Reactome) | |
Integrin alpha 6:beta
4:Plectin complex | Complex | REACT_21067 (Reactome) | |
Integrin alpha 6:beta
4:Plectin:BP180: Laminin-322 complex | Complex | REACT_20915 (Reactome) | |
Integrin alpha6:beta4:
Plectin:BP180 complex | Complex | REACT_21046 (Reactome) | |
Integrin alpha6beta4 | Complex | REACT_14337 (Reactome) | |
Integrin beta-1 | Protein | P05556 (UniProt) | |
JAM-A | Protein | Q9Y624 (UniProt) | |
JAM-A:PAR-aPKC
complex | Complex | REACT_20246 (Reactome) | |
Keratin 5/14 | Unknown | REACT_20869 (Reactome) | |
Laminin-332 | Complex | REACT_20843 (Reactome) | |
MIG-2 | Protein | Q96AC1 (UniProt) | |
MIG-2:
MIGFILIN | Complex | REACT_21097 (Reactome) | |
MIGFILIN:VASP | Complex | REACT_21228 (Reactome) | |
Migfilin | Protein | Q8WUP2 (UniProt) | |
Migfilin:Filamin A:
F-actin | Complex | REACT_20733 (Reactome) | Interaction of Filamin with Migfiln mediates the association with the Migfilin with actin filaments (Tu et al., 2002). |
Necl-1 | Protein | Q8N126 (UniProt) | |
Necl-1/Necl-
2/Necl-3 homodimer | Complex | REACT_19578 (Reactome) | |
Necl-1/Necl-
2/Necl-3 trans homodimer | Complex | REACT_19789 (Reactome) | |
Necl-1:Necl-2 trans
heterodimer | Complex | REACT_20182 (Reactome) | |
Necl-1:Nectin-1 trans
heterodimer | Complex | REACT_19689 (Reactome) | |
Necl-1:Nectin-3
trans heterodimer | Complex | REACT_19782 (Reactome) | |
Necl-2 | Protein | Q9BY67 (UniProt) | |
Necl-5/PVR | Protein | P15151 (UniProt) | |
Necl-5:Nectin-3 trans
heterodimer | Complex | REACT_19715 (Reactome) | |
Nectin | Protein | REACT_20136 (Reactome) | |
Nectin cis-
homodimer | Complex | REACT_19521 (Reactome) | |
Nectin trans
homodimer | Complex | REACT_19779 (Reactome) | |
Nectin-1 | Protein | Q15223-1 (UniProt) | |
Nectin-1 cis
homodimer | Complex | REACT_19460 (Reactome) | |
Nectin-1:Nectin-3
trans heterodimer | Complex | REACT_20025 (Reactome) | |
Nectin-1:Nectin-4
trans heterodimer | Complex | REACT_20421 (Reactome) | |
Nectin-2 cis
homodimer | Complex | REACT_20053 (Reactome) | |
Nectin-2:Nectin-3
transheterodimer | Complex | REACT_20370 (Reactome) | |
Nectin-3 | Protein | Q9NQS3-1 (UniProt) | |
Nectin-3 cis
homodimer | Complex | REACT_19940 (Reactome) | |
Nectin-3:Necl-2 trans
heterodimer | Complex | REACT_19977 (Reactome) | |
Nectin-4 cis
homodimer | Complex | REACT_20206 (Reactome) | |
Nectin:afadin complex | Complex | REACT_20350 (Reactome) | |
PALS1/MPP5 | Protein | Q8N3R9 (UniProt) | |
PARVA | Protein | Q9NVD7 (UniProt) | |
PARVA:Paxillin | Complex | REACT_21170 (Reactome) | |
PARVA:TESK1 | Complex | REACT_21038 (Reactome) | |
PARVB/Affixin | Protein | Q9HBI1 (UniProt) | |
PARVB:alpha actinin | Complex | REACT_21104 (Reactome) | |
PATJ | Protein | Q8NI35 (UniProt) | |
PINCH | Protein | REACT_20717 (Reactome) | |
PINCH-ILK-
parvin complex | Complex | REACT_20853 (Reactome) | |
PINCH1 | Protein | P48059 (UniProt) | |
Par3:Par6:aPKC
complex | Complex | REACT_19423 (Reactome) | |
ParvB/Affixin:
Alpha-Pix | Complex | REACT_20814 (Reactome) | |
Paxillin | Protein | P49023 (UniProt) | |
Plectin 1 | Protein | Q15149 (UniProt) | |
Rsu-1 | Protein | Q15404 (UniProt) | |
Rsu-1:Pinch1
complex | Complex | REACT_20937 (Reactome) | |
Signal regulatory
protein (SIRP) family interactions | Pathway | REACT_23916 (Reactome) | Signal regulatory protein (SIRP)alpha, also known as SHPS-1 or SIRPA or CD172a, is a transmembrane protein expressed mostly on myeloid cells. CD47, a widely expressed transmembrane protein, is a ligand for SIRP alpha, with the two proteins constituting a cell-cell communication system. The interaction of SIRP alpha with CD47 is important for the regulation of migration and phagocytosis. SIRP alpha functions as a docking protein to recruit and activate SHP-1 or SHP-2 at the cell membrane in response to extracellular stimuli. SIRP alpha also binds other intracellular proteins including the adaptor molecules Src kinase-associated protein (SKAP2 SKAP55hom/R), Fyn-binding protein/SLP-76-associated phosphoprotein (FYB/SLAP-130) and the tyrosine kinase PYK2. SIRP alpha also binds the extracellular proteins, surfactant-A (SP-A) and surfactant-D (SP-D). In addition to SIRP alpha there are two closely related proteins in the SIRP family namely SIRP beta and SIRP gamma. These three family proteins show high sequence similarity and similar extracellular structural topology, including three Ig domains, but their ligand binding topology might differ. SIRP beta is expressed on myeloid cells, including monocytes, granulocytes and DCs. A natural ligand for SIRP beta remains unknown; SIRP gamma can bind to CD47 but the binding affinity is lower than that of SIRP alpha. |
TESK1 | Protein | Q15569 (UniProt) | |
Type II
hemidesmosome | Complex | REACT_20848 (Reactome) | |
VASP | Protein | P50552 (UniProt) | |
alpha-
catenin | Protein | P35221 (UniProt) | |
alpha/beta
parvin | Protein | REACT_20989 (Reactome) | |
claudin trans-
homodimer | Complex | REACT_20391 (Reactome) | |
p120
catenin | Protein | O60716 (UniProt) |
Annotated Interactions
No annotated interactions