rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
12
|
pubmed:dateCreated |
2002-9-4
|
pubmed:abstractText |
A genetic screen for synthetic lethal interactions with arf1(-) identified a recessive mutation in TRS130, one of 10 components in the trafficking protein particle (TRAPP) complex (Sacher et al., 2000). As TRS130 is an essential gene, the synthetic lethal allele (trs130-101) is a novel one that requires ARF1 for viability. This allele was found to exhibit no defects in secretory function, i.e. processing of carboxypeptidase Y or invertase. YPT31 and YPT32 were identified in a subsequent screen as high-copy suppressors of arf1(-)trs130-101. Increasing the gene dosage of YPT31/32 also suppressed lethality resulting from deletion of TRS130 or TRS120 but not three other essential TRAPP subunit-encoding genes. Although unable to suppress defects in several alleles of ARF1, increasing the gene dosage of YPT31/32 suppressed the cold sensitivity of gcs1(-), an Arf GTPase-activating protein (GAP). Thus, these genetic interactions provide initial evidence for linkage of Arf and TRAPP signalling and for Ypt31/32 proteins functioning downstream of both components in the TRAPP complex and of Arf signalling via the Gcs1 Arf GAP.
|
pubmed:grant |
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ADP-Ribosylation Factor 1,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GCS1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/GTPase-Activating Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/YPT31 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/YPT32 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Fructofuranosidase,
http://linkedlifedata.com/resource/pubmed/chemical/rab GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/transport protein particle, TRAPP
|
pubmed:status |
MEDLINE
|
pubmed:month |
Sep
|
pubmed:issn |
0749-503X
|
pubmed:author |
|
pubmed:copyrightInfo |
Copyright 2002 John Wiley & Sons, Ltd.
|
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
19
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1075-86
|
pubmed:dateRevised |
2009-7-14
|
pubmed:meshHeading |
pubmed-meshheading:12210902-ADP-Ribosylation Factor 1,
pubmed-meshheading:12210902-Alleles,
pubmed-meshheading:12210902-Carrier Proteins,
pubmed-meshheading:12210902-DNA-Binding Proteins,
pubmed-meshheading:12210902-Fungal Proteins,
pubmed-meshheading:12210902-GTPase-Activating Proteins,
pubmed-meshheading:12210902-Gene Dosage,
pubmed-meshheading:12210902-Gene Expression Regulation, Fungal,
pubmed-meshheading:12210902-Genes, Suppressor,
pubmed-meshheading:12210902-Glycoside Hydrolases,
pubmed-meshheading:12210902-Membrane Proteins,
pubmed-meshheading:12210902-Mutation,
pubmed-meshheading:12210902-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:12210902-Signal Transduction,
pubmed-meshheading:12210902-Vesicular Transport Proteins,
pubmed-meshheading:12210902-Yeasts,
pubmed-meshheading:12210902-beta-Fructofuranosidase,
pubmed-meshheading:12210902-rab GTP-Binding Proteins
|
pubmed:year |
2002
|
pubmed:articleTitle |
Genetic interactions link ARF1, YPT31/32 and TRS130.
|
pubmed:affiliation |
Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322-3050, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|