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

Court, N.W., Ingley, E., Klinken, S.P. and Bogoyevitch, M.A. (2005) Outer membrane protein 25-a mitochondrial anchor and inhibitor of stress-activated protein kinase-3. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1744 (1). pp. 68-75.

Free to read: https://doi.org/10.1016/j.bbamcr.2004.11.008
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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 α1-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 α1-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.

Publication Type: Journal Article
Publisher: Elsevier B.V.
Copyright: © 2004 Elsevier B.V.
URI: http://researchrepository.murdoch.edu.au/id/eprint/39566
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