Source:http://linkedlifedata.com/resource/pubmed/id/12395193
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2002-10-23
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| pubmed:abstractText |
The CGP1 gene was identified in a screen for mutations that were synthetic lethal in combination with a deletion of the gene (CPF1) for centromere and promoter factor 1. Cells deleted for CGP1 showed reduced viability, were temperature sensitive for growth and exhibited altered sensitivity to microtubule-destabilizing drugs. Furthermore, Deltacgp1 cells showed increased rates of loss of a circular minichromosome and defects in the positioning of the short mitotic spindle. Further phenotypic analysis of Deltacgp1 cells revealed that loss of Cgp1p function led to severe depolarization of the actin cytoskeleton. In addition, cells deleted for CGP1 were hypersensitive to the actin-disrupting compound Latrunculin-A, exhibited strongly reduced polarized localization of the unconventional myosin Myo2p, and showed defects in other actin-related processes, such as shmoo formation and cell wall integrity. Cgp1p was recently identified by several groups as Vps54p, which is a member of the VFT complex that is involved in vesicular protein transport at the level of the late Golgi, acting as a tethering factor. Our data show for the first time that Cgp1p/Vps54p links aspects of vesicular protein transport with the organization of the actin cytoskeleton.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Bicyclo Compounds, Heterocyclic,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SAC2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Thiazoles,
http://linkedlifedata.com/resource/pubmed/chemical/Thiazolidines,
http://linkedlifedata.com/resource/pubmed/chemical/VPS54 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/latrunculin A
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| pubmed:status |
MEDLINE
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| pubmed:month |
Oct
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| pubmed:issn |
1617-4615
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
268
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
190-205
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:12395193-Actins,
pubmed-meshheading:12395193-Bicyclo Compounds, Heterocyclic,
pubmed-meshheading:12395193-Cell Wall,
pubmed-meshheading:12395193-Cytoskeleton,
pubmed-meshheading:12395193-Fungal Proteins,
pubmed-meshheading:12395193-Membrane Proteins,
pubmed-meshheading:12395193-Mutation,
pubmed-meshheading:12395193-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:12395193-Thiazoles,
pubmed-meshheading:12395193-Thiazolidines,
pubmed-meshheading:12395193-Two-Hybrid System Techniques,
pubmed-meshheading:12395193-Vesicular Transport Proteins,
pubmed-meshheading:12395193-Yeasts
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| pubmed:year |
2002
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| pubmed:articleTitle |
The vesicular transport protein Cgp1p/Vps54p/Tcs3p/Luv1p is required for the integrity of the actin cytoskeleton.
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| pubmed:affiliation |
Institut für Mikrobiologie, Heinrich-Heine Universität, Universitätsstrasse 1, Geb. 26.12.01.64, 40225 Düsseldorf, Germany.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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