rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
16
|
pubmed:dateCreated |
2010-8-16
|
pubmed:abstractText |
SGs are mRNA containing cytoplasmic structures that are assembled in response to stress. Tudor-SN protein is a ubiquitously expressed protein. Here, Tudor-SN protein was found to physiologically interact with G3BP, which is the marker and effector of SG. The kinetics of the assembly of SGs in the living cells demonstrated that Tudor-SN co-localizes with G3BP and is recruited to the same SGs in response to different stress stimuli. Knockdown of endogenous Tudor-SN did not inhibit the formation of SGs, but retarded the aggregation of small SGs into large SGs. Thus Tudor-SN may not be an initiator as essential as G3BP for the formation of SGs, but affects the aggregation of SGs. These findings identify Tudor-SN as a novel component of SGs.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
1873-3468
|
pubmed:author |
|
pubmed:copyrightInfo |
Copyright 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
|
pubmed:issnType |
Electronic
|
pubmed:day |
20
|
pubmed:volume |
584
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
3525-32
|
pubmed:meshHeading |
pubmed-meshheading:20643132-Animals,
pubmed-meshheading:20643132-COS Cells,
pubmed-meshheading:20643132-Carrier Proteins,
pubmed-meshheading:20643132-Cercopithecus aethiops,
pubmed-meshheading:20643132-Cytoplasmic Granules,
pubmed-meshheading:20643132-Gene Knockdown Techniques,
pubmed-meshheading:20643132-HeLa Cells,
pubmed-meshheading:20643132-Humans,
pubmed-meshheading:20643132-Nuclear Proteins,
pubmed-meshheading:20643132-Protein Interaction Mapping,
pubmed-meshheading:20643132-RNA, Small Interfering,
pubmed-meshheading:20643132-Recombinant Fusion Proteins,
pubmed-meshheading:20643132-Stress, Physiological
|
pubmed:year |
2010
|
pubmed:articleTitle |
Tudor-SN interacts with and co-localizes with G3BP in stress granules under stress conditions.
|
pubmed:affiliation |
Department of Immunology, Basic Medical College, Tianjin Medical University, PR China.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|