Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-8-17
pubmed:databankReference
pubmed:abstractText
The immunosuppressants rapamycin and FK506 bind to the same intracellular protein, the immunophilin FKBP12. The FKB12-FK506 complex interacts with and inhibits the Ca(2+)-activated protein phosphatase calcineurin. The target of the FKBP12-rapamycin complex has not yet been identified. We report that a protein complex containing 245 kDa and 35 kDa components, designated rapamycin and FKBP12 targets 1 and 2 (RAFT1 and RAFT2), interacts with FKBP12 in a rapamycin-dependent manner. Sequences (330 amino acids total) of tryptic peptides derived from the 245 kDa RAFT1 reveal striking homologies to the yeast TOR gene products, which were originally identified by mutations that confer rapamycin resistance in yeast. A RAFT1 cDNA was obtained and found to encode a 289 kDa protein (2549 amino acids) that is 43% and 39% identical to TOR2 and TOR1, respectively. We propose that RAFT1 is the direct target of FKBP12-rapamycin and a mammalian homolog of the TOR proteins.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases (Alcohol Group..., http://linkedlifedata.com/resource/pubmed/chemical/Polyenes, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Sirolimus, http://linkedlifedata.com/resource/pubmed/chemical/Succinimides, http://linkedlifedata.com/resource/pubmed/chemical/TOR Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/TOR1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/TOR2 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Tacrolimus, http://linkedlifedata.com/resource/pubmed/chemical/Tacrolimus Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/disuccinimidyl suberate
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
78
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
35-43
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:7518356-Amino Acid Sequence, pubmed-meshheading:7518356-Animals, pubmed-meshheading:7518356-Base Sequence, pubmed-meshheading:7518356-Brain Chemistry, pubmed-meshheading:7518356-Carrier Proteins, pubmed-meshheading:7518356-Cell Cycle Proteins, pubmed-meshheading:7518356-Cloning, Molecular, pubmed-meshheading:7518356-Cross-Linking Reagents, pubmed-meshheading:7518356-DNA, Complementary, pubmed-meshheading:7518356-Fungal Proteins, pubmed-meshheading:7518356-Heat-Shock Proteins, pubmed-meshheading:7518356-Molecular Sequence Data, pubmed-meshheading:7518356-Phosphatidylinositol 3-Kinases, pubmed-meshheading:7518356-Phosphotransferases (Alcohol Group Acceptor), pubmed-meshheading:7518356-Polyenes, pubmed-meshheading:7518356-Rats, pubmed-meshheading:7518356-Saccharomyces cerevisiae, pubmed-meshheading:7518356-Saccharomyces cerevisiae Proteins, pubmed-meshheading:7518356-Sequence Alignment, pubmed-meshheading:7518356-Sequence Analysis, pubmed-meshheading:7518356-Sequence Homology, Amino Acid, pubmed-meshheading:7518356-Sirolimus, pubmed-meshheading:7518356-Succinimides, pubmed-meshheading:7518356-TOR Serine-Threonine Kinases, pubmed-meshheading:7518356-Tacrolimus, pubmed-meshheading:7518356-Tacrolimus Binding Proteins
pubmed:year
1994
pubmed:articleTitle
RAFT1: a mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs.
pubmed:affiliation
Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't