English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Protein kinase C betaII regulates Akt phosphorylation on Ser-473 in a cell type- and stimulus-specific fashion.

Kawakami, Y., Nishimoto, H., Kitaura, J., Maeda-Yamamoto, M., Kato, R. M., Littman, D. R., et al. (2004). Protein kinase C betaII regulates Akt phosphorylation on Ser-473 in a cell type- and stimulus-specific fashion. Journal of Biological Chemistry, 279(46), 47720-47725. Retrieved from http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15364915.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-EBCE-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-E095-9
Genre: Journal Article

Files

show Files
hide Files
:
270908.pdf (Publisher version), 0B
Name:
270908.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Kawakami, Y., Author
Nishimoto, H., Author
Kitaura, J., Author
Maeda-Yamamoto, M., Author
Kato, R. M., Author
Littman, D. R., Author
Leitges, M.1, Author              
Rawlings, D. J., Author
Kawakami, T., Author
Affiliations:
1Department of Genes and Behavior, MPI for biophysical chemistry, Max Planck Society, ou_persistent34              

Content

show
hide
Free keywords: Animals; Bone Marrow Cells/cytology/physiology; Cells, Cultured; Enzyme Activation; Immunoglobulin E/pharmacology; Interleukin-2/secretion; Isoenzymes/genetics/metabolism Mast Cells/cytology/drug effects/physiology; Mice; Mice, Knockout; Phorbol Esters/pharmacology; Phosphorylation; Protein Kinase C/genetics/metabolism; Protein-Serine-Threonine Kinases/genetics/metabolism; Proto-Oncogene Proteins/genetics/metabolism; Receptors, IgE/metabolism; Research Support, U.S. Gov't, P.H.S.; Serine/metabolism
 Abstract: Akt (= protein kinase B), a subfamily of the AGC serine/threonine kinases, plays critical roles in survival, proliferation, glucose metabolism, and other cellular functions. Akt activation requires the recruitment of the enzyme to the plasma membrane by interacting with membrane-bound lipid products of phosphatidylinositol 3-kinase. Membrane-bound Akt is then phosphorylated at two sites for its full activation; Thr-308 in the activation loop of the kinase domain is phosphorylated by 3-phosphoinositide-dependent kinase-1 (PDK1) and Ser-473 in the C-terminal hydrophobic motif by a putative kinase PDK2. The identity of PDK2 has been elusive. Here we present evidence that conventional isoforms of protein kinase C (PKC), particularly PKCbetaII, can regulate Akt activity by directly phosphorylating Ser-473 in vitro and in IgE/antigen-stimulated mast cells. By contrast, PKCbeta is not required for Ser-473 phosphorylation in mast cells stimulated with stem cell factor or interleukin-3, in serum-stimulated fibroblasts, or in antigen receptor-stimulated T or B lymphocytes. Therefore, PKCbetaII appears to work as a cell type- and stimulus-specific PDK2.

Details

show
hide
Language(s): eng - English
 Dates: 2004-11-12
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of Biological Chemistry
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 279 (46) Sequence Number: - Start / End Page: 47720 - 47725 Identifier: -