Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1999-4-13
pubmed:databankReference
pubmed:abstractText
We have recently isolated a neural tissue-specific syntaxin-1-binding protein, named tomosyn, which is capable of dissociating Munc18/n-Sec1/rbSec1 from syntaxin-1 to form a 10S tomosyn complex, an intermediate complex converted to the 7S SNARE complex. We isolated here two splicing variants of tomosyn: one had 36 amino acids (aa) insertion and another had 17 aa deletion. We named original one m-tomosyn, big one b-tomosyn, and small one s-tomosyn. s-Tomosyn as well as m-tomosyn was mainly expressed in brain whereas b-tomosyn was ubiquitously expressed. All the isoforms bound to syntaxin-1, but not to syntaxin-2, -3, or -4, and had a region highly homologous to VAMP, another syntaxin-binding protein. This region was necessary but not sufficient for high-affinity binding of tomosyn to syntaxin-1.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Surface, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Neuropeptides, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments, http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms, http://linkedlifedata.com/resource/pubmed/chemical/Qa-SNARE Proteins, http://linkedlifedata.com/resource/pubmed/chemical/R-SNARE Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/Stx1a protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Stxbp5 protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Syntaxin 1, http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-291X
pubmed:author
pubmed:copyrightInfo
Copyright 1999 Academic Press.
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
256
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
218-22
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed-meshheading:10066450-Alternative Splicing, pubmed-meshheading:10066450-Amino Acid Sequence, pubmed-meshheading:10066450-Animals, pubmed-meshheading:10066450-Antigens, Surface, pubmed-meshheading:10066450-Base Sequence, pubmed-meshheading:10066450-Brain, pubmed-meshheading:10066450-Carrier Proteins, pubmed-meshheading:10066450-Cloning, Molecular, pubmed-meshheading:10066450-Gene Expression, pubmed-meshheading:10066450-Gene Library, pubmed-meshheading:10066450-Kidney, pubmed-meshheading:10066450-Membrane Proteins, pubmed-meshheading:10066450-Molecular Sequence Data, pubmed-meshheading:10066450-Nerve Tissue Proteins, pubmed-meshheading:10066450-Neuropeptides, pubmed-meshheading:10066450-Organ Specificity, pubmed-meshheading:10066450-Peptide Fragments, pubmed-meshheading:10066450-Polymerase Chain Reaction, pubmed-meshheading:10066450-Protein Binding, pubmed-meshheading:10066450-Protein Isoforms, pubmed-meshheading:10066450-Qa-SNARE Proteins, pubmed-meshheading:10066450-R-SNARE Proteins, pubmed-meshheading:10066450-RNA, Messenger, pubmed-meshheading:10066450-Rats, pubmed-meshheading:10066450-Syntaxin 1, pubmed-meshheading:10066450-Vesicular Transport Proteins
pubmed:year
1999
pubmed:articleTitle
Three splicing variants of tomosyn and identification of their syntaxin-binding region.
pubmed:affiliation
Department of Molecular Biology and Biochemistry, Osaka University Medical School, Suita, 565-0871, Japan.
pubmed:publicationType
Journal Article