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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
35
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pubmed:dateCreated |
1998-9-24
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pubmed:abstractText |
Small Rab GTPases are involved in the regulation of membrane trafficking. They cycle between cytosolic and membrane-bound forms. These membrane association/dissociation are tightly controlled by regulatory proteins. To search for proteins interacting with Rab13, a small GTPase associated with vesicles in fibroblasts and predominantly with tight junctions in epithelial cells, we screened a HeLa two-hybrid cDNA library and isolated a clone encoding a protein of 17.4 kDa. This protein, almost identical to the bovine rod cGMP phosphodiesterase delta subunit, was named human delta-PDE. The delta-PDE binds specifically to Rab13. It exhibits two putative C-terminal sequences necessary for the interaction with PDZ (PSD95, Dlg, ZO-1) domains contained in many proteins localized to specific plasma membrane microdomains. Immunofluorescence microscopic studies revealed that the vesicular stomatitis virus (VSV)-tagged delta-PDE is localized in vesicular structures accumulated near the plasma membrane in epithelial cells. Deletion of the PDZ binding motifs impair VSV-delta-PDE subcellular distribution. Purified recombinant delta-PDE had the capacity to dissociate Rab13 from cellular membranes. Our data support the proposal that delta-PDE, but not GDP dissociation inhibitor, may serve to control the dynamic of the association of Rab13 with cellular membranes.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/3',5'-Cyclic-GMP Phosphodiesterases,
http://linkedlifedata.com/resource/pubmed/chemical/G protein, vesicular stomatitis...,
http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/RAB13 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Envelope Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/rab GTP-Binding Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:volume |
273
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
22340-5
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:9712853-3',5'-Cyclic-GMP Phosphodiesterases,
pubmed-meshheading:9712853-Amino Acid Sequence,
pubmed-meshheading:9712853-Animals,
pubmed-meshheading:9712853-Cattle,
pubmed-meshheading:9712853-Cell Membrane,
pubmed-meshheading:9712853-GTP Phosphohydrolases,
pubmed-meshheading:9712853-GTP-Binding Proteins,
pubmed-meshheading:9712853-HeLa Cells,
pubmed-meshheading:9712853-Humans,
pubmed-meshheading:9712853-LLC-PK1 Cells,
pubmed-meshheading:9712853-Membrane Glycoproteins,
pubmed-meshheading:9712853-Microscopy, Fluorescence,
pubmed-meshheading:9712853-Molecular Sequence Data,
pubmed-meshheading:9712853-Retinal Rod Photoreceptor Cells,
pubmed-meshheading:9712853-Sequence Homology, Amino Acid,
pubmed-meshheading:9712853-Subcellular Fractions,
pubmed-meshheading:9712853-Swine,
pubmed-meshheading:9712853-Viral Envelope Proteins,
pubmed-meshheading:9712853-rab GTP-Binding Proteins
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pubmed:year |
1998
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pubmed:articleTitle |
The rod cGMP phosphodiesterase delta subunit dissociates the small GTPase Rab13 from membranes.
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pubmed:affiliation |
CNRS UMR 144, Compartimentation et Dynamique Cellulaires, Institut Curie, 75248 Paris Cedex 05, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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