A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA turnover by recruiting the degradation machinery

Roberto Gherzi, Kyung Yeol Lee, Paola Briata, Daniel Wegmüller, Christoph Moroni, Michael Karin, Ching Yi Chen

Research output: Contribution to journalArticle

309 Citations (Scopus)

Abstract

Inherently unstable mRNAs contain AU-rich elements (AREs) in their 3′ untranslated regions that act as mRNA stability determinants by interacting with ARE binding proteins (ARE-BPs). The mechanisms underlying the function of ARE and ARE-BP interactions in promoting mRNA decay are not fully understood. Here, we demonstrate that KSRP, a KH domain-containing ARE-BP, is an essential factor for ARE-directed mRNA decay. Some of the KH motifs (KHs) of KSRP directly mediate RNA binding, mRNA decay, and interactions with the exosome and poly(A) ribonuclease (PARN). The ability of KHs to promote mRNA decay correlates with their ability to bind the ARE and associate with RNA-degrading enzymes. Thus, KHs promote rapid mRNA decay by recruiting degradation machinery to ARE-containing mRNAs.

Original languageEnglish
Pages (from-to)571-583
Number of pages13
JournalMolecular Cell
Volume14
Issue number5
DOIs
Publication statusPublished - Jun 4 2004

Fingerprint

AU Rich Elements
RNA Stability
Messenger RNA
RNA
Exosomes
RNA Recognition Motif Proteins
3' Untranslated Regions
Carrier Proteins

ASJC Scopus subject areas

  • Molecular Biology

Cite this

A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA turnover by recruiting the degradation machinery. / Gherzi, Roberto; Lee, Kyung Yeol; Briata, Paola; Wegmüller, Daniel; Moroni, Christoph; Karin, Michael; Chen, Ching Yi.

In: Molecular Cell, Vol. 14, No. 5, 04.06.2004, p. 571-583.

Research output: Contribution to journalArticle

Gherzi, Roberto ; Lee, Kyung Yeol ; Briata, Paola ; Wegmüller, Daniel ; Moroni, Christoph ; Karin, Michael ; Chen, Ching Yi. / A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA turnover by recruiting the degradation machinery. In: Molecular Cell. 2004 ; Vol. 14, No. 5. pp. 571-583.
@article{4f9a7c21de184869b4c34dfe05f038b4,
title = "A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA turnover by recruiting the degradation machinery",
abstract = "Inherently unstable mRNAs contain AU-rich elements (AREs) in their 3′ untranslated regions that act as mRNA stability determinants by interacting with ARE binding proteins (ARE-BPs). The mechanisms underlying the function of ARE and ARE-BP interactions in promoting mRNA decay are not fully understood. Here, we demonstrate that KSRP, a KH domain-containing ARE-BP, is an essential factor for ARE-directed mRNA decay. Some of the KH motifs (KHs) of KSRP directly mediate RNA binding, mRNA decay, and interactions with the exosome and poly(A) ribonuclease (PARN). The ability of KHs to promote mRNA decay correlates with their ability to bind the ARE and associate with RNA-degrading enzymes. Thus, KHs promote rapid mRNA decay by recruiting degradation machinery to ARE-containing mRNAs.",
author = "Roberto Gherzi and Lee, {Kyung Yeol} and Paola Briata and Daniel Wegm{\"u}ller and Christoph Moroni and Michael Karin and Chen, {Ching Yi}",
year = "2004",
month = "6",
day = "4",
doi = "10.1016/j.molcel.2004.05.002",
language = "English",
volume = "14",
pages = "571--583",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "5",

}

TY - JOUR

T1 - A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA turnover by recruiting the degradation machinery

AU - Gherzi, Roberto

AU - Lee, Kyung Yeol

AU - Briata, Paola

AU - Wegmüller, Daniel

AU - Moroni, Christoph

AU - Karin, Michael

AU - Chen, Ching Yi

PY - 2004/6/4

Y1 - 2004/6/4

N2 - Inherently unstable mRNAs contain AU-rich elements (AREs) in their 3′ untranslated regions that act as mRNA stability determinants by interacting with ARE binding proteins (ARE-BPs). The mechanisms underlying the function of ARE and ARE-BP interactions in promoting mRNA decay are not fully understood. Here, we demonstrate that KSRP, a KH domain-containing ARE-BP, is an essential factor for ARE-directed mRNA decay. Some of the KH motifs (KHs) of KSRP directly mediate RNA binding, mRNA decay, and interactions with the exosome and poly(A) ribonuclease (PARN). The ability of KHs to promote mRNA decay correlates with their ability to bind the ARE and associate with RNA-degrading enzymes. Thus, KHs promote rapid mRNA decay by recruiting degradation machinery to ARE-containing mRNAs.

AB - Inherently unstable mRNAs contain AU-rich elements (AREs) in their 3′ untranslated regions that act as mRNA stability determinants by interacting with ARE binding proteins (ARE-BPs). The mechanisms underlying the function of ARE and ARE-BP interactions in promoting mRNA decay are not fully understood. Here, we demonstrate that KSRP, a KH domain-containing ARE-BP, is an essential factor for ARE-directed mRNA decay. Some of the KH motifs (KHs) of KSRP directly mediate RNA binding, mRNA decay, and interactions with the exosome and poly(A) ribonuclease (PARN). The ability of KHs to promote mRNA decay correlates with their ability to bind the ARE and associate with RNA-degrading enzymes. Thus, KHs promote rapid mRNA decay by recruiting degradation machinery to ARE-containing mRNAs.

UR - http://www.scopus.com/inward/record.url?scp=2942612333&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=2942612333&partnerID=8YFLogxK

U2 - 10.1016/j.molcel.2004.05.002

DO - 10.1016/j.molcel.2004.05.002

M3 - Article

C2 - 15175153

AN - SCOPUS:2942612333

VL - 14

SP - 571

EP - 583

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 5

ER -