Statements in which the resource exists as a subject.
PredicateObject
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: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