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Outer membrane protein 25-a mitochondrial anchor and inhibitor of stress-activated protein kinase-3
Journal article   Peer reviewed

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

N.W. Court, E. Ingley, S.P. Klinken and M.A. Bogoyevitch
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, Vol.1744(1), pp.68-75
2005
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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.

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Citation topics
1 Clinical & Life Sciences
1.25 Molecular & Cell Biology - Cancer, Autophagy & Apoptosis
1.25.887 RAS
Web Of Science research areas
Biochemistry & Molecular Biology
Cell Biology
ESI research areas
Molecular Biology & Genetics
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