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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
2003-11-25
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pubmed:abstractText |
Neo1p from Saccharomyces cerevisiae is an essential P-type ATPase and potential aminophospholipid translocase (flippase) in the Drs2p family. We have previously implicated Drs2p in protein transport steps in the late secretory pathway requiring ADP-ribosylation factor (ARF) and clathrin. Here, we present evidence that epitope-tagged Neo1p localizes to the endoplasmic reticulum (ER) and Golgi complex and is required for a retrograde transport pathway between these organelles. Using conditional alleles of NEO1, we find that loss of Neo1p function causes cargo-specific defects in anterograde protein transport early in the secretory pathway and perturbs glycosylation in the Golgi complex. Rer1-GFP, a protein that cycles between the ER and Golgi complex in COPI and COPII vesicles, is mislocalized to the vacuole in neo1-ts at the nonpermissive temperature. These phenotypes suggest that the anterograde protein transport defect is a secondary consequence of a defect in a COPI-dependent retrograde pathway. We propose that loss of lipid asymmetry in the cis Golgi perturbs retrograde protein transport to the ER.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12960419-10429211,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12960419-10601336,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/12960419-9927415
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1059-1524
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
14
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4971-83
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:12960419-Adenosine Triphosphatases,
pubmed-meshheading:12960419-Amino Acid Sequence,
pubmed-meshheading:12960419-COP-Coated Vesicles,
pubmed-meshheading:12960419-Cell Membrane Structures,
pubmed-meshheading:12960419-Cloning, Molecular,
pubmed-meshheading:12960419-Endoplasmic Reticulum,
pubmed-meshheading:12960419-Glycosylation,
pubmed-meshheading:12960419-Golgi Apparatus,
pubmed-meshheading:12960419-Membrane Proteins,
pubmed-meshheading:12960419-Membrane Transport Proteins,
pubmed-meshheading:12960419-Microscopy, Electron,
pubmed-meshheading:12960419-Models, Molecular,
pubmed-meshheading:12960419-Molecular Sequence Data,
pubmed-meshheading:12960419-Protein Transport,
pubmed-meshheading:12960419-Saccharomyces cerevisiae,
pubmed-meshheading:12960419-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:12960419-Vacuoles
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pubmed:year |
2003
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pubmed:articleTitle |
Requirement for neo1p in retrograde transport from the Golgi complex to the endoplasmic reticulum.
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pubmed:affiliation |
Department of Biological Sciences, Vanderbilt University, Nashville, Tennessee 37235-1634, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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