Interaction between PAK and nck: a template for Nck targets and role of PAK autophosphorylation.

Interaction between PAK and nck: a template for Nck targets and role of PAK autophosphorylation. Research Abstract Details 

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Interaction between PAK and nck: a template for Nck targets and role of PAK autophosphorylation. Abstract Text:

Z S Zhao,E Manser,L Lim,

The kinase PAK binds tightly to the SH3 domain of its partner PIX via a central proline-rich sequence. A different N-terminal sequence allows alphaPAK to bind an SH3 domain of the adaptor Nck. The Nck SH3[2] domain interacts equally with an 18-mer PAK-derived peptide and full-length alphaPAK. Detailed analysis of this binding by saturation substitution allows related Nck targets to be accurately identified from sequence characteristics alone. All Nck SH3[2] binding proteins, including PAK, NIK, synaptojanin, PRK2, and WIP, possess the motif PXXPXRXXS; in the case of PAK, serine phosphorylation at this site negatively regulates binding. We show that kinase autophosphorylation blocks binding by both Nck and PIX to alphaPAK, thus providing a mechanism to regulate PAK interactions with its SH3-containing partners. One cellular consequence of the regulatable binding of PAK is facilitation of its cycling between cytosolic and focal complex sites.

Interaction between PAK and nck: a template for Nck targets and role of PAK autophosphorylation. Publishing Authors By Initials

ZS Zhao,E Manser,L Lim,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: molecular structure: molecular conformation: protein conformation: protein structure, tertiary: protein interaction domains and motifs: src homology domains research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: molecular structure: molecular conformation: protein conformation: protein structure, tertiary: protein interaction domains and motifs: src homology domains research

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Interaction between PAK and nck: a template for Nck targets and role of PAK autophosphorylation. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Molecular and cellular biology

VOLUME: 20

Page Numbers: 3906-17

Journal Abbreviation: Mol. Cell. Biol.

ISSN: 0270-7306

DAY: 19

MONTH: Jun

YEAR: 2000

Interaction between PAK and nck: a template for Nck targets and role of PAK autophosphorylation. Information

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LANGUAGE: eng

NlmUniqueID: 8109087

Interaction between PAK and nck: a template for Nck targets and role of PAK autophosphorylation. Keywords Mesh Terms:

KEYWORDS: src Homology Domains

MESH TERMS: metabolism

Chemical & Substance for Abstract: Interaction between PAK and nck: a template for Nck targets and role of PAK autophosphorylation. Information

Substance Name: p21-Activated Kinases

Registry Number: EC 2.7.11.1

Grant and Affiliation Information for Interaction between PAK and nck: a template for Nck targets and role of PAK autophosphorylation.

AFFILIATION: Glaxo-IMCB Group, Institute of Molecular & Cell Biology, Singapore 117609, Singapore.

Country: UNITED STATES

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MEDLINETA: Mol Cell Biol

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