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Description |
Simple eukaryotes such as yeasts and molds encode multiple PAKs (p21-Activated
Kinases) that, like their orthologs in other systems, act downstream of
Rho-family GTPases. All PAKs contain an N-terminal PBD (p21
GTPase-Binding-Domain), which confers binding to small GTPases such as CDC42
(Cell Division Cycle-42) or Rac, and a C-terminal protein kinase
domain, but they do not bind to Rho, Ras, or other small G-proteins. CDC42
and Rac bind in a GTP-dependent fashion to a highly conserved
sequence, referred to as the CRIB (CDC42 and Rac Interactive Binding) domain,
found in the N-terminal regulatory domains of all characterized PAKs
(Ref.1).
The fission yeast Schizosaccharomyces pombe encodes two
PAK kinases–Pak1/Shk1 and Pak2/Shk2–both of which, like their counterparts in
budding yeast regulate of MAPK [...] |
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References:
1. Shk1, a homolog of the Saccharomyces cerevisiae Ste20 and mammalian p65PAK protein kinases, is a component of a Ras/Cdc42 signaling module in the fission yeast Schizosaccharomyces pombe.Marcus S, Polverino A, Chang E, Robbins D, Cobb MH, Wigler MH.Proc Natl Acad Sci U S A. 1995 Jun 20; 92(13):6180-4.2. The highly conserved SKB1 gene encodes a protein that interacts with Shk1, a fission yeast Ste20/PAK homolog.Gilbreth M, Yang P, Wang D, Frost J, Polverino A, Cobb MH, Marcus S.Proc Natl Acad Sci U S A. 1996 Nov 26; 93(24):13802-7.
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