Gene interactions and pathways from curated databases and text-mining

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CAV1 — FYN

Pathways - manually collected, often from reviews:

  • BioCarta integrin signaling pathway: ECM/Integrin-alpha/Integrin-beta/Caveolin-1/FYN complex (CAV1-ITGB1-ITGA1-FYN) → SHC/GRB2/SOS-1 complex (SOS1-GRB2-SHC1) (modification, activates)
  • BioCarta integrin signaling pathway: ECM/Integrin-alpha/Integrin-beta/Caveolin-1/FYN complex (CAV1-ITGB1-ITGA1-FYN) (modification, collaborate)
  • BioCarta integrin signaling pathway: ECM/Integrin-alpha/Integrin-beta/Caveolin-1/FYN complex (CAV1-ITGB1-ITGA1-FYN) → Integrin-alpha/Integrin-beta/Caveolin-1/FYN complex (FYN-ITGB1-ITGA1-CAV1) (modification, collaborate)
  • BioCarta integrin signaling pathway: ECM () → Integrin-alpha/Integrin-beta/Caveolin-1/FYN complex (FYN-ITGB1-ITGA1-CAV1) (modification, collaborate)
  • KEGG Focal adhesion: CAV1/CAV2/CAV3 → FYN (protein-protein, activation)
  • KEGG Viral myocarditis: FYN → CAV1 (protein-protein, activation)
  • WikiPathways Focal Adhesion: CAV1/CAV3/CAV2 → FYN (activation)

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

Text-mined interactions from Literome

Mouillet-Richard et al., Science 2000 : A caveolin-1 dependent coupling of PrPc to the tyrosine kinase Fyn was observed
Kellermann et al., C R Biol 2002 : The coupling of PrPc to Fyn is dependent on caveolin-1
Kawabe et al., Am J Physiol Heart Circ Physiol 2004 : Taken together, caveolin in caveolae may keep ERK inactive, but when caveolin is translocated to noncaveolar sites in response to stretch stress, caveolin mediates stretch induced ERK activation through an association with beta1-integrins/Fyn/Shc
Ramos et al., Anticancer Res 2011 (Carcinoma, Squamous Cell...) : The tumor promoter/suppressor caveolin-1 , which associates with MT1-MMP, also requires FYN activation for expression
Shi et al., Med Microbiol Immunol 2013 : With deleted and inserted PrP mutants within octarepeat region, we observed obvious octarepeat associated phenomena, including lower binding capacity with Cav-1 in vitro, unable to co-localize with Cav-1 in the cells and to induce up-regulation of p-Cav-1 and p-Fyn when removal of octarepeats in the context of full-length PrP
Mastick et al., J Biol Chem 1997 : In adipocytes, overexpression of wild type Fyn leads to increased basal phosphorylation of caveolin and hyperphosphorylation of caveolin in response to insulin