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 journalArticlepeer-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 languageEnglish (US)
Pages (from-to)1735-1736
Number of pages2
JournalEMBO Journal
Volume33
Issue number16
DOIs
StatePublished - 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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