Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
30
pubmed:dateCreated
1996-9-3
pubmed:databankReference
pubmed:abstractText
Despite the central role vesicular trafficking occupies in protein targeting, the molecular coding of the trafficking signals and the mechanism of vesicle docking and fusion are just beginning to be understood. We report here the cloning and initial characterization of a new member of the syntaxin family of vesicular transport receptors. Syntaxin 6 is a 255-amino acid protein with two domains predicted to form coiled-coils, as well as a carboxyl-terminal membrane anchor. Syntaxin 6 is broadly expressed and localizes in the region of the Golgi apparatus. In vitro binding studies established that syntaxin 6 binds to alpha-soluble NSF attachment protein (alpha-SNAP). The sequence homology, topology, localization, and alpha-SNAP binding suggest that syntaxin 6 is involved in intracellular vesicle trafficking.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
17961-5
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:8663448-Biological Transport, pubmed-meshheading:8663448-Carrier Proteins, pubmed-meshheading:8663448-Cell Compartmentation, pubmed-meshheading:8663448-DNA, Complementary, pubmed-meshheading:8663448-Golgi Apparatus, pubmed-meshheading:8663448-Intracellular Membranes, pubmed-meshheading:8663448-Membrane Proteins, pubmed-meshheading:8663448-Molecular Sequence Data, pubmed-meshheading:8663448-Multigene Family, pubmed-meshheading:8663448-Protein Binding, pubmed-meshheading:8663448-Protein Structure, Secondary, pubmed-meshheading:8663448-Qa-SNARE Proteins, pubmed-meshheading:8663448-RNA, pubmed-meshheading:8663448-Sequence Analysis, DNA, pubmed-meshheading:8663448-Soluble N-Ethylmaleimide-Sensitive Factor Attachment..., pubmed-meshheading:8663448-Tissue Distribution, pubmed-meshheading:8663448-Vesicular Transport Proteins
pubmed:year
1996
pubmed:articleTitle
A new syntaxin family member implicated in targeting of intracellular transport vesicles.
pubmed:affiliation
Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Stanford University Medical Center, California 94305-5428, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't