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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1997-2-27
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pubmed:abstractText |
The localization of proteins to late-Golgi membranes (TGN) of Saccharomyces cerevisiae is conferred by targeting motifs containing aromatic residues in the cytosolic domains of these proteins. These signals could act by directing retrieval from a post-Golgi compartment or by preventing exit from the TGN. To investigate the mechanism of localization of yeast TGN proteins, we used the heterologous protein A-ALP (consisting of the cytosolic domain of dipeptidyl aminopeptidase A [DPAP A] fused to the transmembrane and luminal domains of the vacuolar protein alkaline phosphatase [ALP]), which localizes to the yeast TGN. Insertion of the aromatic residue-based TGN localization motif (FXFXD) of DPAP A into the cytosolic domain of ALP results in a protein that resides in the TGN. We demonstrate that the FXFXD motif confers Golgi localization through retrieval from a post-Golgi compartment by detecting a post-Golgi processed form of this protein in the TGN. We present an assay that uncouples retrieval-mediated Golgi localization from static retention-based localization, allowing measurement of the rate at which proteins exit the yeast TGN. We also demonstrate that the cytosolic domain of DPAP A contains additional information, separate from the retrieval motif, that slows exit from the TGN. We propose a model for DPAP A localization that involves two distinct mechanisms: one in which the FXFXD motif directs retrieval from a post-Golgi compartment, and a second that slows the rate at which DPAP A exits the TGN.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-1310258,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-1323236,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-1385813,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-1469044,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-14731888,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-1493334,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-1493335,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-1498362,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-1527174,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-1655802,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-1812718,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-1848556,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-1918142,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-1935889,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-1935890,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-1986005,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-2016334,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-2071670,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-2676517,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-3323813,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-7490293,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-7499343,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-7579696,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-7588625,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-7593183,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-7698993,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-7720726,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-7781597,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-7957057,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-7969419,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-8144594,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-8187177,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-8226795,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-8242736,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-8308064,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-8308065,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-8362242,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-8370450,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-8392934,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-8400455,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-8436587,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-8491209,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-8509444,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-8534908,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-8599108,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-8601597,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-8636229,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-8649377,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9015300-8730101
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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 |
Jan
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pubmed:issn |
0021-9525
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
136
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
287-97
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:9015300-Alkaline Phosphatase,
pubmed-meshheading:9015300-Cell Compartmentation,
pubmed-meshheading:9015300-Cytosol,
pubmed-meshheading:9015300-Fungal Proteins,
pubmed-meshheading:9015300-Golgi Apparatus,
pubmed-meshheading:9015300-Membrane Proteins,
pubmed-meshheading:9015300-Peptidyl-Dipeptidase A,
pubmed-meshheading:9015300-Protein Sorting Signals,
pubmed-meshheading:9015300-Recombinant Fusion Proteins,
pubmed-meshheading:9015300-Saccharomyces cerevisiae,
pubmed-meshheading:9015300-Vacuoles
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pubmed:year |
1997
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pubmed:articleTitle |
Two separate signals act independently to localize a yeast late Golgi membrane protein through a combination of retrieval and retention.
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pubmed:affiliation |
Institute of Molecular Biology, University of Oregon, Eugene 97403-1229, USA.
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pubmed:publicationType |
Journal Article
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