Formation of the PINCH-ILK-parvin complex

Stable Identifier
Reaction [binding]
Homo sapiens
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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).

Literature References
PubMed ID Title Journal Year
11331308 A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading

Huang, Y, Zhang, Y, Tu, Y, Wu, C, Hua, Y

J Cell Biol 2001
Orthologous Events
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