rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
2
|
pubmed:dateCreated |
2002-1-11
|
pubmed:abstractText |
The regulation of membrane traffic involves the Rab family of Ras-related GTPases, of which there are a total of 11 members in the yeast Saccharomyces cerevisiae. Previous work has identified PRA1 as a dual prenylated Rab GTPase and VAMP2 interacting protein [Martinic et al. (1999) J. Biol. Chem. 272, 26991-26998]. In this study we demonstrate that the yeast counterpart of PRA1 interacts with Rab proteins and with Yip1p, a membrane protein of unknown function that has been reported to interact specifically with the Rab proteins Ypt1p and Ypt31p. Yeast Pra1p/Yip3p is a factor capable of biochemical interaction with a panel of different Rab proteins and does not show in vitro specificity for any particular Rab. The interactions between Pra1p/Yip3p and Rab proteins are dependent on the presence of the Rab protein C-terminal cysteines and require C-terminal prenylation.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion 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/Yip1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/rab GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/rab1 GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/rab5 GTP-Binding Proteins
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
0006-291X
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
18
|
pubmed:volume |
290
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
676-81
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading |
pubmed-meshheading:11785952-Blotting, Western,
pubmed-meshheading:11785952-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:11785952-Fungal Proteins,
pubmed-meshheading:11785952-Membrane Proteins,
pubmed-meshheading:11785952-Protein Binding,
pubmed-meshheading:11785952-Receptors, Cell Surface,
pubmed-meshheading:11785952-Recombinant Fusion Proteins,
pubmed-meshheading:11785952-Saccharomyces cerevisiae,
pubmed-meshheading:11785952-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11785952-Two-Hybrid System Techniques,
pubmed-meshheading:11785952-Vesicular Transport Proteins,
pubmed-meshheading:11785952-rab GTP-Binding Proteins,
pubmed-meshheading:11785952-rab1 GTP-Binding Proteins,
pubmed-meshheading:11785952-rab5 GTP-Binding Proteins
|
pubmed:year |
2002
|
pubmed:articleTitle |
Saccharomyces cerevisiae Pra1p/Yip3p interacts with Yip1p and Rab proteins.
|
pubmed:affiliation |
Department of Molecular Medicine, Cornell University, Ithaca, New York 14853-6401, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|