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 journalArticle

1 Citation (Scopus)

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

Fingerprint

Inhibitor of Apoptosis Proteins
Ubiquitination
Ubiquitin
Mitogen-Activated Protein Kinases
Phosphotransferases
Chemical activation
Apoptosis
Proteins

ASJC Scopus subject areas

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

Cite this

ERK5 signaling gets XIAPed : A role for ubiquitin in the disassembly of a MAPK cascade. / Klein, Aileen M.; Cobb, Melanie H.

In: EMBO Journal, Vol. 33, No. 16, 18.08.2014, p. 1735-1736.

Research output: Contribution to journalArticle

@article{8bc14a17c2d94502b70a79749a62279a,
title = "ERK5 signaling gets XIAPed: A role for ubiquitin in the disassembly of a MAPK cascade",
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.",
author = "Klein, {Aileen M.} and Cobb, {Melanie H.}",
year = "2014",
month = "8",
day = "18",
doi = "10.15252/embj.201489205",
language = "English (US)",
volume = "33",
pages = "1735--1736",
journal = "EMBO Journal",
issn = "0261-4189",
publisher = "Nature Publishing Group",
number = "16",

}

TY - JOUR

T1 - ERK5 signaling gets XIAPed

T2 - A role for ubiquitin in the disassembly of a MAPK cascade

AU - Klein, Aileen M.

AU - Cobb, Melanie H.

PY - 2014/8/18

Y1 - 2014/8/18

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84905718045&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84905718045&partnerID=8YFLogxK

U2 - 10.15252/embj.201489205

DO - 10.15252/embj.201489205

M3 - Article

VL - 33

SP - 1735

EP - 1736

JO - EMBO Journal

JF - EMBO Journal

SN - 0261-4189

IS - 16

ER -