Outer membrane protein 25-a mitochondrial anchor and inhibitor of stress-activated protein kinase-3

N.W. Court, Evan Ingley, Peter Klinken, M.A. Bogoyevitch

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Stress-activated protein kinase-3 (SAPK3) is unique amongst the mitogen-activated protein kinase (MAPK) family with its C-terminal 5 amino acids directing interaction with the PDZ domain-containing substrates alpha 1-Syntrophin and SAP90/PSD95. Here, we identify three additional PDZ domain-containing binding partners, Lin-7C, Scribble, and outer membrane protein 25 (OMP25). This latter protein is localised together with SAPK3 at the mitochondria but it is not a SAPK3 substrate. Instead, OMP25 inhibits SAPK3 activity towards PDZ domain-containing substrates such as alpha 1-Syntrophin and substrates without PDZ domains such as the mitochondrial protein Sab. This is a new mechanism for the regulation of SAPK3 and suggests that its intracellular activity should not be solely assessed by its phosphorylation status. (c) 2004 Elsevier B.V. All rights reserved.
Original languageEnglish
Pages (from-to)68-75
JournalBIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
Volume1744
Issue number1
DOIs
Publication statusPublished - 2005

Fingerprint Dive into the research topics of 'Outer membrane protein 25-a mitochondrial anchor and inhibitor of stress-activated protein kinase-3'. Together they form a unique fingerprint.

  • Cite this