Linked Life Data

19070363

Source:http://linkedlifedata.com/resource/pubmed/id/19070363

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2009-3-9
pubmed:abstractText
Transient receptor potential canonical (TRPC) channels function as cation channels. In a previous study, we identified the molecular determinants involved in promoting TRPC subunit assembly. In the present study, we used size-exclusion chromatography assays to show that the N-terminus of TRPC4 can self-associate and form a tetramer in cellulo. We further showed that the N-terminus of TRPC4 self-associates via the ankyrin repeat domain and the region downstream from the coiled-coil domain. GST pull-down, yeast two-hybrid, and circular dichroism approaches demonstrated that both domains can self-associate. These findings indicated that the self-association of two distinct domains in the N-terminus of TRPC4 is involved in the assembly of the tetrameric channel.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1532-1991
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
45
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
251-9
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
The self-association of two N-terminal interaction domains plays an important role in the tetramerization of TRPC4.
pubmed:affiliation
Department of Pharmacology, Université de Sherbrooke, Sherbrooke, Quebec, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't