Pep12p is a Multifunctional Yeast Syntaxin that Controls Entry of Biosynthetic, Endocytic and Retrograde Traffic into the Prevacuolar Compartment
Delivery of proteins to the vacuole of the yeast Saccharomyces cerevisiae requires the function of the endosomal syntaxin, Pep12p. Many vacuolar proteins, such as the soluble vacuolar hydrolase, carboxypeptidase Y (CPY), traverse the prevacuolar compartment (PVC) en route to the vacuole. Here we sho...
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| Veröffentlicht in: | Traffic (Copenhagen, Denmark) Denmark), 2000-03, Vol.1 (3), p.259-269 |
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| creator | Gerrard, Sonja R. Levi, Boaz P. Stevens, Tom H. |
| description | Delivery of proteins to the vacuole of the yeast Saccharomyces cerevisiae requires the function of the endosomal syntaxin, Pep12p. Many vacuolar proteins, such as the soluble vacuolar hydrolase, carboxypeptidase Y (CPY), traverse the prevacuolar compartment (PVC) en route to the vacuole. Here we show that deletion of the carboxy‐terminal transmembrane domain of Pep12p results in a temperature‐conditional block in transport of CPY to the PVC. The PVC also receives traffic from the early endosome and the vacuole, and mutation in PEP12 also blocks these other trafficking pathways into the PVC. Therefore, Pep12p is a multifunctional syntaxin that is required for all known trafficking pathways into the yeast PVC. Finally, we found that the internalized pheromone receptor, Ste3p, can cycle out of the PVC in a VPS27‐independent fashion. |
| doi_str_mv | 10.1034/j.1600-0854.2000.010308.x |
| format | Article |
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Many vacuolar proteins, such as the soluble vacuolar hydrolase, carboxypeptidase Y (CPY), traverse the prevacuolar compartment (PVC) en route to the vacuole. Here we show that deletion of the carboxy‐terminal transmembrane domain of Pep12p results in a temperature‐conditional block in transport of CPY to the PVC. The PVC also receives traffic from the early endosome and the vacuole, and mutation in PEP12 also blocks these other trafficking pathways into the PVC. Therefore, Pep12p is a multifunctional syntaxin that is required for all known trafficking pathways into the yeast PVC. Finally, we found that the internalized pheromone receptor, Ste3p, can cycle out of the PVC in a VPS27‐independent fashion.</description><subject>Carboxypeptidase C</subject><subject>endosome</subject><subject>endosomes</subject><subject>Endosomes - metabolism</subject><subject>Fungal Proteins - physiology</subject><subject>hydrolase</subject><subject>Membrane Fusion</subject><subject>Membrane Proteins - metabolism</subject><subject>Membrane Proteins - physiology</subject><subject>Models, Biological</subject><subject>Mutation</subject><subject>Organelles - metabolism</subject><subject>Pheromone receptors</subject><subject>prevacuole</subject><subject>Protein Transport - physiology</subject><subject>Qa-SNARE Proteins</subject><subject>Receptors, Cell Surface - metabolism</subject><subject>Receptors, G-Protein-Coupled</subject><subject>Receptors, Mating Factor</subject><subject>Receptors, Pheromone</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae - ultrastructure</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>SNARE</subject><subject>SNARE Proteins</subject><subject>Syntaxin</subject><subject>Temperature</subject><subject>Transmembrane domains</subject><subject>vacuole</subject><subject>Vacuoles</subject><subject>Vacuoles - metabolism</subject><subject>Vesicular Transport Proteins</subject><issn>1398-9219</issn><issn>1600-0854</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc9u1DAQxiMEon_gFZC5IA7dMHacxDmhsipQqRVVWQ6cLMc7pl4lcWo7sHkM3hhvd1VuiNOMPv_mG9tflr2mkFMo-LtNTiuABYiS5wwAckgyiHz7JDt-PHma-qIRi4bR5ig7CWGTSFZy_jw7opSBoNAcZ79vcKRsJDYQRa6nLlozDTpaN6iOfEcVIvk6D1Ft7UDinYpk6YboXRfIRaozcYZ8sC4k5A6j1WdJXjs9p5aoYU1uMcE_vFojWXllTJLtEF2yQnLj8afSk-uUT679qHzscYgvsmdGdQFfHupp9u3jxWr5eXH15dPl8vxqoXlZpGdxY5gQtK2aCotWcYoaWAUlo61Q0Bgt0Gje6qqqBUUsq7qsTJE-BqBhSIvT7M3ed_TufsIQZW-Dxq5TA7opyJqVdcV5ncC3_wQpEyWIJl0moc0e1d6F4NHI0dte-VlSkLvo5EbuApK7gOQuOrmPTm7T7KvDmqntcf138pBVAt7vgV-2w_n_neXq9vyhLf4A6wepIQ</recordid><startdate>200003</startdate><enddate>200003</enddate><creator>Gerrard, Sonja R.</creator><creator>Levi, Boaz P.</creator><creator>Stevens, Tom H.</creator><general>Blackwell Publishing Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>M7N</scope><scope>7X8</scope></search><sort><creationdate>200003</creationdate><title>Pep12p is a Multifunctional Yeast Syntaxin that Controls Entry of Biosynthetic, Endocytic and Retrograde Traffic into the Prevacuolar Compartment</title><author>Gerrard, Sonja R. ; Levi, Boaz P. ; Stevens, Tom H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4538-94ff2881b696e3ba41ec0260521b8a09fc8efc4bc66781ee56756f38540092e13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Carboxypeptidase C</topic><topic>endosome</topic><topic>endosomes</topic><topic>Endosomes - metabolism</topic><topic>Fungal Proteins - physiology</topic><topic>hydrolase</topic><topic>Membrane Fusion</topic><topic>Membrane Proteins - metabolism</topic><topic>Membrane Proteins - physiology</topic><topic>Models, Biological</topic><topic>Mutation</topic><topic>Organelles - metabolism</topic><topic>Pheromone receptors</topic><topic>prevacuole</topic><topic>Protein Transport - physiology</topic><topic>Qa-SNARE Proteins</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>Receptors, G-Protein-Coupled</topic><topic>Receptors, Mating Factor</topic><topic>Receptors, Pheromone</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae - ultrastructure</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>SNARE</topic><topic>SNARE Proteins</topic><topic>Syntaxin</topic><topic>Temperature</topic><topic>Transmembrane domains</topic><topic>vacuole</topic><topic>Vacuoles</topic><topic>Vacuoles - metabolism</topic><topic>Vesicular Transport Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gerrard, Sonja R.</creatorcontrib><creatorcontrib>Levi, Boaz P.</creatorcontrib><creatorcontrib>Stevens, Tom H.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>Traffic (Copenhagen, Denmark)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gerrard, Sonja R.</au><au>Levi, Boaz P.</au><au>Stevens, Tom H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Pep12p is a Multifunctional Yeast Syntaxin that Controls Entry of Biosynthetic, Endocytic and Retrograde Traffic into the Prevacuolar Compartment</atitle><jtitle>Traffic (Copenhagen, Denmark)</jtitle><addtitle>Traffic</addtitle><date>2000-03</date><risdate>2000</risdate><volume>1</volume><issue>3</issue><spage>259</spage><epage>269</epage><pages>259-269</pages><issn>1398-9219</issn><eissn>1600-0854</eissn><abstract>Delivery of proteins to the vacuole of the yeast Saccharomyces cerevisiae requires the function of the endosomal syntaxin, Pep12p. Many vacuolar proteins, such as the soluble vacuolar hydrolase, carboxypeptidase Y (CPY), traverse the prevacuolar compartment (PVC) en route to the vacuole. Here we show that deletion of the carboxy‐terminal transmembrane domain of Pep12p results in a temperature‐conditional block in transport of CPY to the PVC. The PVC also receives traffic from the early endosome and the vacuole, and mutation in PEP12 also blocks these other trafficking pathways into the PVC. Therefore, Pep12p is a multifunctional syntaxin that is required for all known trafficking pathways into the yeast PVC. Finally, we found that the internalized pheromone receptor, Ste3p, can cycle out of the PVC in a VPS27‐independent fashion.</abstract><cop>Copenhagen</cop><pub>Blackwell Publishing Ltd</pub><pmid>11208109</pmid><doi>10.1034/j.1600-0854.2000.010308.x</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Wiley Free Content |
| subjects | Carboxypeptidase C endosome endosomes Endosomes - metabolism Fungal Proteins - physiology hydrolase Membrane Fusion Membrane Proteins - metabolism Membrane Proteins - physiology Models, Biological Mutation Organelles - metabolism Pheromone receptors prevacuole Protein Transport - physiology Qa-SNARE Proteins Receptors, Cell Surface - metabolism Receptors, G-Protein-Coupled Receptors, Mating Factor Receptors, Pheromone Saccharomyces cerevisiae Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae - ultrastructure Saccharomyces cerevisiae Proteins SNARE SNARE Proteins Syntaxin Temperature Transmembrane domains vacuole Vacuoles Vacuoles - metabolism Vesicular Transport Proteins |
| title | Pep12p is a Multifunctional Yeast Syntaxin that Controls Entry of Biosynthetic, Endocytic and Retrograde Traffic into the Prevacuolar Compartment |
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