ERK5 signaling gets XIAPed: A role for ubiquitin in the disassembly of a MAPK cascade

Aileen M. Klein; Melanie H. Cobb

doi:10.15252/embj.201489205

ERK5 signaling gets XIAPed: A role for ubiquitin in the disassembly of a MAPK cascade

Aileen M. Klein, Melanie H. Cobb

Research output: Contribution to journal › Article › peer-review

1 Scopus citations

Abstract

Mitogen-activated protein kinase (MAPK) cascades are tightly controlled through a series of well-characterized phospho-regulatory events. In this issue, Takeda et al () identify the inhibitor of apoptosis protein, XIAP, as a key regulator of ERK5 activation via uncoupling of upstream kinase activity by non-degradative ubiquitination. The inhibitor of apoptosis (IAP) family proteins is identified as suppressors of MAPK signaling. Mechanistically, IAPs function as upstream kinase uncoupler by virtue of non-degradative ubiquitination.

Original language	English (US)
Pages (from-to)	1735-1736
Number of pages	2
Journal	EMBO Journal
Volume	33
Issue number	16
DOIs	https://doi.org/10.15252/embj.201489205
State	Published - Aug 18 2014

ASJC Scopus subject areas

Neuroscience(all)
Molecular Biology
Biochemistry, Genetics and Molecular Biology(all)
Immunology and Microbiology(all)

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ERK5 signaling gets XIAPed: A role for ubiquitin in the disassembly of a MAPK cascade

Abstract

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