Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
29
pubmed:dateCreated
2008-12-1
pubmed:abstractText
Cytokine-induced suppressor of cytokine signaling (SOCS) proteins function as feedback inhibitors of cytokine receptor signaling by inhibiting the Janus kinase-signal transducer and activator of transcription (JAK-STAT) signal transduction pathway. In this report, microtubule-associated protein 1S (MAP1), a member of the MAP1 family, was identified as a novel SOCS3 interacting protein. MAP1S could bind with microtubules and actin, and decorated and stabilized microtubules. A perinuclear co-localization was discovered between MAP1S and SOCS3. In MAP1S deficient macrophages, inhibition of SOCS3 on STAT3 phosphorylation can be partially hindered in the presence of interleukin-6 (IL-6) and lipopolysaccharide (LPS). The microtubule-depolymerizing drug nocodazole also disrupted the inhibitory activity of the SOCS3 protein. These results suggest that the interaction of SOCS3 with MAP1S and the integrity of the microtubule cytoskeleton play an important role in the negative regulation of SOCS3 on IL-6 signaling.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
582
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4015-22
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
The role of microtubule-associated protein 1S in SOCS3 regulation of IL-6 signaling.
pubmed:affiliation
State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, Hubei 430072, PR China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't