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First published online April 5, 2006
doi: 10.1242/10.1242/jcs.02925

Journal of Cell Science 119, 1469-1475 (2006)
Published by The Company of Biologists 2006
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The multifunctional GIT family of proteins

Ryan J. Hoefen and Bradford C. Berk*

Cardiovascular Research Institute and Department of Medicine, University of Rochester School of Medicine and Dentistry, Rochester, NY 14642, USA


Figure 1
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  		Fig. 1. GIT1 and GIT2 domain structure. The full-length GIT proteins have an N-terminal ARF GTPase-activating protein (ARF-GAP) domain, three ankyrin (ANK) repeats, a Spa2-homology domain (SHD), a coiled-coil (CC) domain and a paxillin-binding site (PBS). The truncated GIT2-short protein lacks the CC domain and PBS.

 

Figure 2
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  		Fig. 2. Summary of GIT1 protein interactions and functions. Major signaling pathways include (A) agonist (Ag)-receptor (GPCR) endocytosis; (B) angiotensin-II (AngII)-stimulated PLC{gamma} activation and Ca2+ mobilization; (C) scaffolding MEK1 activation in response to TRK activation; (D) cytoskeletal regulation through PAK and Rho-family GTPases; and (E) focal complex assembly and disassembly. G, heterotrimeric G proteins; GRK, GPCR kinase; GPCR, G-protein-coupled receptor; IP3, inositol (1,4,5)-trisphosphate; P, phosphorylation; TKR, tyrosine kinase receptor.

 

Figure 3
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  		Fig. 3. Rac1/Cdc42-stimulated PAK activation requires GIT-PIX oligomers. Activated Rac1 and Cdc42 interact with inactive PAK, causing a conformational change that allows it to bind to GIT-PIX oligomers through a direct interaction with PIX. High local concentrations of PAK permit autophosphorylation (P), stimulating the kinase activity of PAK and its subsequent disassociation from the GIT-PIX oligomers.

 




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