Posttranslational control of HuR function

The RNA‐binding protein HuR (human antigen R) associates with numerous transcripts, coding and noncoding, and controls their splicing, localization, stability, and translation. Through its regulation of target transcripts, HuR has been implicated in cellular events including proliferation, senescenc...

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Vydáno v:Wiley interdisciplinary reviews. RNA Ročník 8; číslo 1; s. np - n/a
Hlavní autoři: Grammatikakis, Ioannis, Abdelmohsen, Kotb, Gorospe, Myriam
Médium: Journal Article
Jazyk:angličtina
Vydáno: Hoboken, USA John Wiley & Sons, Inc 01.01.2017
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Témata:
Animals
Apoptosis
Cancer
ELAV-Like Protein 1 - genetics
ELAV-Like Protein 1 - metabolism
Gene expression
Gene Expression Regulation
Humans
HuR protein
Immune response
Localization
Phosphorylation
Protein Processing, Post-Translational - genetics
Proteins
Proteolysis
Ribonucleic acid
RNA
RNA, Messenger - genetics
RNA, Messenger - metabolism
RNA-binding protein
Senescence
Splicing
Ubiquitination
ISSN:1757-7004, 1757-7012, 1757-7012
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Popis
Shrnutí:The RNA‐binding protein HuR (human antigen R) associates with numerous transcripts, coding and noncoding, and controls their splicing, localization, stability, and translation. Through its regulation of target transcripts, HuR has been implicated in cellular events including proliferation, senescence, differentiation, apoptosis, and the stress and immune responses. In turn, HuR influences processes such as cancer and inflammation. HuR function is primarily regulated through posttranslational modifications that alter its subcellular localization and its ability to bind target RNAs; such modifications include phosphorylation, methylation, ubiquitination, NEDDylation, and proteolytic cleavage. In this review, we describe the modifications that impact upon HuR function on gene expression programs and disease states. WIREs RNA 2017, 8:e1372. doi: 10.1002/wrna.1372 This article is categorized under: RNA Interactions with Proteins and Other Molecules > Protein–RNA Recognition RNA Interactions with Proteins and Other Molecules > RNA–Protein Complexes
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ISSN:1757-7004
1757-7012
1757-7012
DOI:10.1002/wrna.1372