PMID- 10075701
OWN - NLM
STAT- MEDLINE
DCOM- 19990415
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 12
DP  - 1999 Mar 19
TI  - Multisite autophosphorylation of p21-activated protein kinase gamma-PAK as a
      function of activation.
PG  - 8022-8
AB  - p21-activated protein kinase (PAK) is a family of serine/threonine kinases whose 
      activity is stimulated by binding to small G-proteins such as Cdc42 and
      subsequent autophosphorylation. Focusing on the ubiquitous gamma-isoform of PAK
      in this study, baculovirus-infected insect cells were used to obtain recombinant 
      gamma-PAK, while native gamma-PAK was isolated from rabbit reticulocytes.
      Two-dimensional gel electrophoresis of gamma-PAK followed by immunoblot analysis 
      revealed a similar profile for native and recombinant gamma-PAK, both consisting 
      of multiple protein spots. Following Cdc42-stimulated autophosphorylation, the
      two-dimensional profiles of native and recombinant gamma-PAK were characterized
      by a similar acidic shift, suggesting a common response to Cdc42. To understand
      the effect of differential phosphorylation on its activation status, gamma-PAK
      autophosphorylation was conducted in the presence or absence of activators such
      as Cdc42 and histone II-AS, followed by tryptic digestion and comparative
      two-dimensional phosphopeptide mapping. The major phosphopeptides were subjected 
      to a combination of manual and automated amino acid sequencing. Overall, eight
      autophosphorylation sites were identified in Cdc42-activated gamma-PAK, six of
      which are in common with those previously reported in alpha-PAK, while Ser-19 and
      Ser-165 appear to be uniquely phosphorylated in the gamma-form. Further, the
      phosphorylation of Ser-141, Ser-165, and Thr-402 was found to correlate with
      gamma-PAK activation.
FAU - Gatti, A
AU  - Gatti A
AD  - Department of Biochemistry, University of California, Riverside, California
      92521, USA.
FAU - Huang, Z
AU  - Huang Z
FAU - Tuazon, P T
AU  - Tuazon PT
FAU - Traugh, J A
AU  - Traugh JA
LA  - eng
GR  - GM26738/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Cell Cycle Proteins)
RN  - 0 (Phosphopeptides)
RN  - 37589-80-3 (Guanosine 5'-O-(3-Thiotriphosphate))
RN  - EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
RN  - EC 2.7.11.1 (p21-Activated Kinases)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
RN  - EC 3.6.5.2 (cdc42 GTP-Binding Protein, Saccharomyces cerevisiae)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Cell Cycle Proteins/metabolism
MH  - GTP-Binding Proteins/metabolism
MH  - Guanosine 5'-O-(3-Thiotriphosphate)/metabolism
MH  - Molecular Sequence Data
MH  - Peptide Mapping
MH  - Phosphopeptides/chemistry
MH  - Phosphorylation
MH  - Protein-Serine-Threonine Kinases/*metabolism
MH  - Rabbits
MH  - Sequence Alignment
MH  - cdc42 GTP-Binding Protein, Saccharomyces cerevisiae
MH  - p21-Activated Kinases
EDAT- 1999/03/13 00:00
MHDA- 1999/03/13 00:01
CRDT- 1999/03/13 00:00
PHST- 1999/03/13 00:00 [pubmed]
PHST- 1999/03/13 00:01 [medline]
PHST- 1999/03/13 00:00 [entrez]
AID - 10.1074/jbc.274.12.8022 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Mar 19;274(12):8022-8. doi: 10.1074/jbc.274.12.8022.