DAZAP1 interacts via its RNA-recognition motifs with the C-termini of other RNA-binding proteins

Huei-Ting Yang; Mark Peggie; Philip Cohen; Simon Rousseau

doi:10.1016/j.bbrc.2009.01.166

DAZAP1 interacts via its RNA-recognition motifs with the C-termini of other RNA-binding proteins

Huei-Ting Yang, Mark Peggie, Philip Cohen, Simon Rousseau

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

18 Citations (Scopus)

Abstract

The turnover and translation of many human mRNAs is regulated by AU-rich elements present in their 3'-untranslated region, which bind various trans acting factors. We previously identified a trans acting factor that interacts with these cis elements as DAZAP1 (deleted in Azoospermia (DAZ)-Associated Protein 1), whose interaction with the germ cell-specific protein DAZ was disrupted by the phosphorylation of DAZAP1. Here we have identified several other RNA-binding proteins as binding partners for DAZAP1 in non-germinal cells. Unlike DAZ, these interactions Occur between the RNA recognition motifs of DAZAP1 and the C-termini of the binding partners and in a phosphorylation-independent manner. The results suggest that DAZAP1 is a component of complexes that are crucial for the degradation and silencing of mRNA. (C) 2009 Elsevier Inc. All rights reserved.

Original language	English
Pages (from-to)	705-709
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	380
Issue number	3
DOIs	https://doi.org/10.1016/j.bbrc.2009.01.166
Publication status	Published - 13 Mar 2009

Keywords

mRNA
AU-rich element
hnRNP
Translation
Protein-protein interaction
ALPHA MESSENGER-RNA
3' UNTRANSLATED REGION
AU-RICH ELEMENTS
HNRNP A1
DECAY
DEGRADATION
KSRP
HUR
PHOSPHORYLATION
IDENTIFICATION

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10.1016/j.bbrc.2009.01.166

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title = "DAZAP1 interacts via its RNA-recognition motifs with the C-termini of other RNA-binding proteins",

abstract = "The turnover and translation of many human mRNAs is regulated by AU-rich elements present in their 3'-untranslated region, which bind various trans acting factors. We previously identified a trans acting factor that interacts with these cis elements as DAZAP1 (deleted in Azoospermia (DAZ)-Associated Protein 1), whose interaction with the germ cell-specific protein DAZ was disrupted by the phosphorylation of DAZAP1. Here we have identified several other RNA-binding proteins as binding partners for DAZAP1 in non-germinal cells. Unlike DAZ, these interactions Occur between the RNA recognition motifs of DAZAP1 and the C-termini of the binding partners and in a phosphorylation-independent manner. The results suggest that DAZAP1 is a component of complexes that are crucial for the degradation and silencing of mRNA. (C) 2009 Elsevier Inc. All rights reserved.",

keywords = "mRNA, AU-rich element, hnRNP, Translation, Protein-protein interaction, ALPHA MESSENGER-RNA, 3' UNTRANSLATED REGION, AU-RICH ELEMENTS, HNRNP A1, DECAY, DEGRADATION, KSRP, HUR, PHOSPHORYLATION, IDENTIFICATION",

author = "Huei-Ting Yang and Mark Peggie and Philip Cohen and Simon Rousseau",

year = "2009",

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doi = "10.1016/j.bbrc.2009.01.166",

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T1 - DAZAP1 interacts via its RNA-recognition motifs with the C-termini of other RNA-binding proteins

AU - Yang, Huei-Ting

AU - Peggie, Mark

AU - Cohen, Philip

AU - Rousseau, Simon

PY - 2009/3/13

Y1 - 2009/3/13

N2 - The turnover and translation of many human mRNAs is regulated by AU-rich elements present in their 3'-untranslated region, which bind various trans acting factors. We previously identified a trans acting factor that interacts with these cis elements as DAZAP1 (deleted in Azoospermia (DAZ)-Associated Protein 1), whose interaction with the germ cell-specific protein DAZ was disrupted by the phosphorylation of DAZAP1. Here we have identified several other RNA-binding proteins as binding partners for DAZAP1 in non-germinal cells. Unlike DAZ, these interactions Occur between the RNA recognition motifs of DAZAP1 and the C-termini of the binding partners and in a phosphorylation-independent manner. The results suggest that DAZAP1 is a component of complexes that are crucial for the degradation and silencing of mRNA. (C) 2009 Elsevier Inc. All rights reserved.

AB - The turnover and translation of many human mRNAs is regulated by AU-rich elements present in their 3'-untranslated region, which bind various trans acting factors. We previously identified a trans acting factor that interacts with these cis elements as DAZAP1 (deleted in Azoospermia (DAZ)-Associated Protein 1), whose interaction with the germ cell-specific protein DAZ was disrupted by the phosphorylation of DAZAP1. Here we have identified several other RNA-binding proteins as binding partners for DAZAP1 in non-germinal cells. Unlike DAZ, these interactions Occur between the RNA recognition motifs of DAZAP1 and the C-termini of the binding partners and in a phosphorylation-independent manner. The results suggest that DAZAP1 is a component of complexes that are crucial for the degradation and silencing of mRNA. (C) 2009 Elsevier Inc. All rights reserved.

KW - mRNA

KW - AU-rich element

KW - hnRNP

KW - Translation

KW - Protein-protein interaction

KW - ALPHA MESSENGER-RNA

KW - 3' UNTRANSLATED REGION

KW - AU-RICH ELEMENTS

KW - HNRNP A1

KW - DECAY

KW - DEGRADATION

KW - KSRP

KW - HUR

KW - PHOSPHORYLATION

KW - IDENTIFICATION

U2 - 10.1016/j.bbrc.2009.01.166

DO - 10.1016/j.bbrc.2009.01.166

M3 - Article

C2 - 19285026

SN - 0006-291X

VL - 380

SP - 705

EP - 709

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 3

ER -

DAZAP1 interacts via its RNA-recognition motifs with the C-termini of other RNA-binding proteins

Abstract

Keywords

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