Medical Journals

A Wd-fyve Protein Binds to the Kinases Akt and Pkczeta/Lambda.

Authors:
  • Fritzius Thorsten
  • Burkard Gabriela
  • Haas Elvira
  • Heinrich Jochen
  • Schweneker Marc
  • Bosse Magnus
  • Zimmermann Sven
  • Frey Alexander D
  • Caelers Antje
  • Bachmann Andre S
  • Moelling Karin

From: Institute of Medical Virology, University of Zurich, Gloriastrasse 30, CH-8006 Zurich, Switzerland.

The Biochemical journal

  • Publish Date: Oct 2006
  • ISSN: 1470-8728
  • Volume: 399
  • Issue: 1
  • Pages: 9-20
  • Medium: Internet
  • Language: English
  • Citation (JAMA): Fritzius Thorsten, Burkard Gabriela, Haas Elvira, et al. A Wd-fyve Protein Binds to the Kinases Akt and Pkczeta/Lambda.. Biochem. J. Oct 2006;399:9-20

Abstract

WD (tryptophan-aspartic acid dipeptide)-repeat proteins play a central role in signal transduction cascades by co-ordinating the interaction of key signalling molecules. We identified a novel propeller-FYVE [domain identified in Fab1p, YOTB, Vac1p and EEA1 (early endosome antigen 1)] protein, ProF, which is expressed in various cell lines and tissues and consists of seven WD-repeats and a FYVE domain. WD-repeat proteins offer a platform for protein-protein interactions by folding into a seven-bladed propeller-like structure, while the FYVE domain binds to phosphatidylinositol 3-phosphate present mainly on intracellular membranes. The ProF protein partially co-localizes with EEA1 on vesicular structures and binds to the protein kinases Akt and PKCzeta/lambda (protein kinase Czeta/lambda) via its WD-repeat propeller. ProF interacts more strongly with the kinases after hormonal stimulation. Endogenously expressed ProF and the two kinases interact in brain and in the preadipocyte cell line 3T3-L1, suggesting a role in secretory vesicular processes. In summary, we describe a new binding partner for kinases, located on vesicular structures in specialized cells, which may play a role for the spatial organization of signalling cascades.

Mesh Headings (Keywords): Amino Acid Sequence, Animals, Carrier Proteins, Cell Line, Cercopithecus aethiops, Humans, Intracellular Signaling Peptides and Proteins, Isoenzymes, Mice, Molecular Sequence Data, Oncogene Protein v-akt, Protein Conformation, Protein Kinase C, Protein Structure, Tertiary, Rats, Signal Transduction


Check for Full Text / PubMed Unique Identifier (PMID): 16792529


This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.

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The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.


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