How signaling proteins integrate multiple inputs: A comparison of N-WASP and Cdk2

Current Opinion in Cell Biology

Volumn 14, Issue 2, 2002, Pages 149-154

  Prehoda, Kenneth E ^a,b   Lim, Wendell A ^a,b  

^a UNIVERSITY OF OREGON   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CYCLIN A; CYCLIN DEPENDENT KINASE 2; PROTEIN CDC42; WISKOTT ALDRICH SYNDROME PROTEIN;

CELL FUNCTION; COMPARATIVE STUDY; HUMAN; PHOSPHORYLATION; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN BINDING; REVIEW; SIGNAL TRANSDUCTION;

EID: 0036531884     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(02)00307-1     Document Type: Review

References (23)

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6. Signalling to actin: The Cdc42-N-WASP-Arp2/3 connection
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8. The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly
9. Mechanism of N-WASP activation by Cdc42 and phosphatidylinositol 4,5-bisphosphate
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12. Nck and phosphatidylinositol 4,5-bisphosphate synergistically activate actin polymerization through the N-WASP-Arp2/3 pathway
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20. The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases
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23. Effects of phosphorylation by CAK on cyclin binding by CDC2 and CDK2