PAK1 binds RAC1:GTP

Stable Identifier
Reaction [binding]
Homo sapiens
Locations in the PathwayBrowser
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

Serine/threonine-protein kinase PAK1 (PAK1) exists as homodimer in a trans-inhibited conformation. PAK1 translocates from cytosol to plasma membrane and comes in close proximity to RAC1. The kinase inhibitory (KI) domain of one PAK1 molecule binds to the C-terminal catalytic domain of the other and inhibits catalytic activity. RAC1:GTP bind to the GBD domain of PAK1 thereby altering the conformation of the KI domain, relieving inhibition of its catalytic domain, and allowing PAK1 autophosphorylation that is required for full kinase activity (Parrini et al. 2002, Zhao & Manser 2005, Sells et al. 2000).

Literature References
PubMed ID Title Journal Year
11804587 Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1

Parrini, MC, Lei, M, Mayer, BJ, Harrison, SC

Mol Cell 2002
15548136 PAK and other Rho-associated kinases--effectors with surprisingly diverse mechanisms of regulation

Manser, E, Zhao, ZS

Biochem J 2005
11134074 Temporal and spatial distribution of activated Pak1 in fibroblasts

Pfaff, A, Chernoff, J, Sells, MA

J. Cell Biol. 2000
Orthologous Events
Cite Us!