Interaction between PAK and Nck: a Template for Nck Targets and Role of PAK Autophosphorylation
American Society for Microbiology, 2000
Online
unknown
Zugriff:
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.
Titel: |
Interaction between PAK and Nck: a Template for Nck Targets and Role of PAK Autophosphorylation
|
---|---|
Autor/in / Beteiligte Person: | Manser, Edward ; Zhao, Zhou-shen ; Lim, Louis |
Link: | |
Veröffentlichung: | American Society for Microbiology, 2000 |
Medientyp: | unknown |
Schlagwort: |
|
Sonstiges: |
|