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A brain serine/threonine protein kinase activated by Cdc42 and Rac1
- E. Manser, T. Leung, Harfizah Salihuddin, Zhuo-shen Zhao, L. Lim
- Biology, ChemistryNature
- 6 January 1994
A new brain serine/threonine protein kinase may be a target for the p21 ras -related proteins Cdc42 and Rac1, and provides a model for studying p21 regulation of mammalian phosphorylation signalling pathways.
PAK kinases are directly coupled to the PIX family of nucleotide exchange factors.
The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton
The multidomained ROK alpha appears to be involved in reorganization of the cytoskeleton, with the N and C termini acting as positive and negative regulators, respectively, of the kinase domain whose activity is crucial for formation of stress fibers and focal adhesion complexes.
The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts
It is shown that microinjection of the related human Cdc42Hs into Swiss 3T3 fibroblasts induced the formation of peripheral actin microspikes, determined by staining with phalloidin, and that Cdc 42Hs plays an important role in determining mammalian cell morphology.
Expression of constitutively active alpha-PAK reveals effects of the kinase on actin and focal complexes
Transfection shows that in epithelial HeLa cells alpha-PAK is recruited from the cytoplasm to distinct focal complexes by both Cdc42(G 12V) and Rac1(G12V), which themselves colocalize to these sites, which support previous suggestions of a role for PAK downstream of both CDC42 and Rac 1 and indicate that PAK functions include the dissolution of stress fibers and reorganization of focal complexes.
Coupling of PAK-Interacting Exchange Factor PIX to GIT1 Promotes Focal Complex Disassembly
- Zhou-shen Zhao, E. Manser, T. Loo, L. Lim
- Biology, ChemistryMolecular and Cellular Biology
- 1 September 2000
It is proposed that GIT1 and FAK cooperate to promote motility both by directly regulating focal complex dynamics and by the activation of Rac.
A Novel Serine/Threonine Kinase Binding the Ras-related RhoA GTPase Which Translocates the Kinase to Peripheral Membranes (*)
- T. Leung, E. Manser, L. Tan, L. Lim
- Biology, ChemistryThe Journal of Biological Chemistry
- 8 December 1995
The isolation of a rat cDNA encoding a 150-kDa protein, which specifically binds RhoA in its GTP form and contains an N-terminal serine/threonine kinase domain highly related to the human myotonic dystrophy kinase and a cysteine-rich domain toward the C terminus is reported.
Pak Functions Downstream of Dock to Regulate Photoreceptor Axon Guidance in Drosophila
Rho family GTPases and neuronal growth cone remodelling: relationship between increased complexity induced by Cdc42Hs, Rac1, and acetylcholine and collapse induced by RhoA and lysophosphatidic acid
There is competition between the ACh- and LPA-induced morphological pathways mediated by Cdc42Hs and/or Rac1 and by RhoA, leading to either neurite development or collapse in N1E-115 neuroblastoma growth cones.
A Conserved Negative Regulatory Region in αPAK: Inhibition of PAK Kinases Reveals Their Morphological Roles Downstream of Cdc42 and Rac1
- Zhou-shen Zhao, E. Manser, Xiang-qun Chen, Claire Chong, T. Leung, L. Lim
- BiologyMolecular and Cellular Biology
- 1 April 1998
These results, coupled with previous observations with constitutively active PAK, demonstrate that these kinases play an important role downstream of Cdc42 and Rac1 in cytoskeletal reorganization.