Linked Life Data

9015300

Source:http://linkedlifedata.com/resource/pubmed/id/9015300

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pubmed-article:9015300pubmed:abstractTextThe 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.lld:pubmed
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pubmed-article:9015300pubmed:authorpubmed-author:BryantN JNJlld:pubmed
pubmed-article:9015300pubmed:authorpubmed-author:StevensT HTHlld:pubmed
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pubmed-article:9015300pubmed:pagination287-97lld:pubmed
pubmed-article:9015300pubmed:dateRevised2009-11-18lld:pubmed
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pubmed-article:9015300pubmed:year1997lld:pubmed
pubmed-article:9015300pubmed:articleTitleTwo separate signals act independently to localize a yeast late Golgi membrane protein through a combination of retrieval and retention.lld:pubmed
pubmed-article:9015300pubmed:affiliationInstitute of Molecular Biology, University of Oregon, Eugene 97403-1229, USA.lld:pubmed
pubmed-article:9015300pubmed:publicationTypeJournal Articlelld:pubmed
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