The yeast v-SNARE Vti1p mediates two vesicle transport pathways through interactions with the t-SNAREs Sed5p and Pep12p
Membrane traffic in eukaryotic cells requires that specific v-SNAREs on transport vesicles interact with specific t-SNAREs on target membranes. We identified a novel Saccharomyces cerevisiae v-SNARE (Vti1p) encoded by the essential gene, VTI1. Vti1p interacts with the prevacuolar t-SNARE Pep12p to d...
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| Veröffentlicht in: | The Journal of cell biology 1997-06, Vol.137 (7), p.1511-1524 |
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| creator | Von Mollard, G.F. (University of Oregon, Eugene, OR.) Nothwehr, S.F Stevens, T.H |
| description | Membrane traffic in eukaryotic cells requires that specific v-SNAREs on transport vesicles interact with specific t-SNAREs on target membranes. We identified a novel Saccharomyces cerevisiae v-SNARE (Vti1p) encoded by the essential gene, VTI1. Vti1p interacts with the prevacuolar t-SNARE Pep12p to direct Golgi to prevacuolar traffic. vti1-1 mutant cells missorted and secreted the soluble vacuolar hydrolase carboxypeptidase Y (CPY) rapidly and reversibly when vti1-1 cells were shifted to the restrictive temperature. However, overexpression of Pep12p suppressed the CPY secretion defect exhibited by vti1-1 cells at 36 degrees C. Characterization of a second vti1 mutant, vti1-11, revealed that Vti1p also plays a role in membrane traffic at a cis-Golgi stage. vti1 -11 mutant cells displayed a growth defect and accumulated the ER and early Golgi forms of both CPY and the secreted protein invertase at the nonpermissive temperature. Overexpression of the yeast cis-Golgi t-SNARE Sed5p suppressed the accumulation of the ER form of CPY but did not lead to CPY transport to the vacuole in vti1-11 cells. Overexpression of Sed5p allowed growth in the absence of Vti1p. In vitro binding and coimmunoprecipitation studies revealed that Vti1p interacts directly with the two t-SNAREs, Sed5p and Pep12p. These data suggest that Vti1p plays a role in cis-Golgi membrane traffic, which is essential for yeast viability, and a nonessential role in the fusion of Golgi-derived vesicles with the prevacuolar compartment. Therefore, a single v-SNARE can interact functionally with two different t-SNAREs in directing membrane traffic in yeast |
| doi_str_mv | 10.1083/jcb.137.7.1511 |
| format | Article |
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(University of Oregon, Eugene, OR.) ; Nothwehr, S.F ; Stevens, T.H</creator><creatorcontrib>Von Mollard, G.F. (University of Oregon, Eugene, OR.) ; Nothwehr, S.F ; Stevens, T.H</creatorcontrib><description>Membrane traffic in eukaryotic cells requires that specific v-SNAREs on transport vesicles interact with specific t-SNAREs on target membranes. We identified a novel Saccharomyces cerevisiae v-SNARE (Vti1p) encoded by the essential gene, VTI1. Vti1p interacts with the prevacuolar t-SNARE Pep12p to direct Golgi to prevacuolar traffic. vti1-1 mutant cells missorted and secreted the soluble vacuolar hydrolase carboxypeptidase Y (CPY) rapidly and reversibly when vti1-1 cells were shifted to the restrictive temperature. However, overexpression of Pep12p suppressed the CPY secretion defect exhibited by vti1-1 cells at 36 degrees C. Characterization of a second vti1 mutant, vti1-11, revealed that Vti1p also plays a role in membrane traffic at a cis-Golgi stage. vti1 -11 mutant cells displayed a growth defect and accumulated the ER and early Golgi forms of both CPY and the secreted protein invertase at the nonpermissive temperature. Overexpression of the yeast cis-Golgi t-SNARE Sed5p suppressed the accumulation of the ER form of CPY but did not lead to CPY transport to the vacuole in vti1-11 cells. Overexpression of Sed5p allowed growth in the absence of Vti1p. In vitro binding and coimmunoprecipitation studies revealed that Vti1p interacts directly with the two t-SNAREs, Sed5p and Pep12p. These data suggest that Vti1p plays a role in cis-Golgi membrane traffic, which is essential for yeast viability, and a nonessential role in the fusion of Golgi-derived vesicles with the prevacuolar compartment. Therefore, a single v-SNARE can interact functionally with two different t-SNAREs in directing membrane traffic in yeast</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.137.7.1511</identifier><identifier>PMID: 9199167</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>AMINO ACID SEQUENCES ; Amino acids ; APARATO GOLGI ; APPAREIL DE GOLGI ; BETA-FRUCTOFURANOSIDASE ; BINDING PROTEINS ; Biological transport ; Biological Transport - genetics ; CARBOXYPEPTIDASES ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Cell growth ; CELL MEMBRANES ; Cells ; Cellular biology ; CHEMICAL COMPOSITION ; COMPOSICION QUIMICA ; COMPOSITION CHIMIQUE ; Cytoplasmic Granules - genetics ; Cytoplasmic Granules - metabolism ; CYTOPLASMIC ORGANELLES ; FRUCTOFURANOSIDASA ; FRUCTOFURANOSIDASE ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; GENBANK/AF00674 ; Gene Expression Regulation, Fungal ; Genes ; GOLGI APPARATUS ; IMMUNOCYTOCHEMISTRY ; IMMUNOLOGIE ; IMMUNOLOGY ; INMUNOLOGIA ; MEMBRANAS CELULARES ; MEMBRANE CELLULAIRE ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; MEMBRANE VESICLES ; Membranes ; METABOLISME DES PROTEINES ; METABOLISMO PROTEICO ; MOLECULAR SEQUENCE DATA ; MUTANT ; MUTANTES ; MUTANTS ; ORGANITE CELLULAIRE ; ORGANULOS CITOPLASMICOS ; PEPTIDASAS ; PEPTIDASE ; PEPTIDASES ; Plasmids ; PROTEIN METABOLISM ; PROTEIN TRANSPORT ; PROTEINAS ; PROTEINAS AGLUTINANTES ; PROTEINE ; PROTEINE DE LIAISON ; PROTEINS ; Qa-SNARE Proteins ; Qb-SNARE Proteins ; REGULATION ; SACCHAROMYCES CEREVISIAE ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae - ultrastructure ; Saccharomyces cerevisiae Proteins ; SECRECION ; SECRETION ; Traffic ; Transport vesicles ; VACUOLA ; VACUOLE ; VACUOLES ; Vesicular Transport Proteins ; Yeast ; Yeasts</subject><ispartof>The Journal of cell biology, 1997-06, Vol.137 (7), p.1511-1524</ispartof><rights>Copyright 1997 The Rockefeller University Press</rights><rights>Copyright Rockefeller University Press Jun 30, 1997</rights><rights>1997</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c486t-1385444ff1c41262a20c380591f2ade19cb8ba8085470a9b3f1b34c9e5c3cc953</citedby><cites>FETCH-LOGICAL-c486t-1385444ff1c41262a20c380591f2ade19cb8ba8085470a9b3f1b34c9e5c3cc953</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,778,782,883,27913,27914</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9199167$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Von Mollard, G.F. (University of Oregon, Eugene, OR.)</creatorcontrib><creatorcontrib>Nothwehr, S.F</creatorcontrib><creatorcontrib>Stevens, T.H</creatorcontrib><title>The yeast v-SNARE Vti1p mediates two vesicle transport pathways through interactions with the t-SNAREs Sed5p and Pep12p</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>Membrane traffic in eukaryotic cells requires that specific v-SNAREs on transport vesicles interact with specific t-SNAREs on target membranes. We identified a novel Saccharomyces cerevisiae v-SNARE (Vti1p) encoded by the essential gene, VTI1. Vti1p interacts with the prevacuolar t-SNARE Pep12p to direct Golgi to prevacuolar traffic. vti1-1 mutant cells missorted and secreted the soluble vacuolar hydrolase carboxypeptidase Y (CPY) rapidly and reversibly when vti1-1 cells were shifted to the restrictive temperature. However, overexpression of Pep12p suppressed the CPY secretion defect exhibited by vti1-1 cells at 36 degrees C. Characterization of a second vti1 mutant, vti1-11, revealed that Vti1p also plays a role in membrane traffic at a cis-Golgi stage. vti1 -11 mutant cells displayed a growth defect and accumulated the ER and early Golgi forms of both CPY and the secreted protein invertase at the nonpermissive temperature. Overexpression of the yeast cis-Golgi t-SNARE Sed5p suppressed the accumulation of the ER form of CPY but did not lead to CPY transport to the vacuole in vti1-11 cells. Overexpression of Sed5p allowed growth in the absence of Vti1p. In vitro binding and coimmunoprecipitation studies revealed that Vti1p interacts directly with the two t-SNAREs, Sed5p and Pep12p. These data suggest that Vti1p plays a role in cis-Golgi membrane traffic, which is essential for yeast viability, and a nonessential role in the fusion of Golgi-derived vesicles with the prevacuolar compartment. Therefore, a single v-SNARE can interact functionally with two different t-SNAREs in directing membrane traffic in yeast</description><subject>AMINO ACID SEQUENCES</subject><subject>Amino acids</subject><subject>APARATO GOLGI</subject><subject>APPAREIL DE GOLGI</subject><subject>BETA-FRUCTOFURANOSIDASE</subject><subject>BINDING PROTEINS</subject><subject>Biological transport</subject><subject>Biological Transport - genetics</subject><subject>CARBOXYPEPTIDASES</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell growth</subject><subject>CELL MEMBRANES</subject><subject>Cells</subject><subject>Cellular biology</subject><subject>CHEMICAL COMPOSITION</subject><subject>COMPOSICION QUIMICA</subject><subject>COMPOSITION CHIMIQUE</subject><subject>Cytoplasmic Granules - genetics</subject><subject>Cytoplasmic Granules - metabolism</subject><subject>CYTOPLASMIC ORGANELLES</subject><subject>FRUCTOFURANOSIDASA</subject><subject>FRUCTOFURANOSIDASE</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>GENBANK/AF00674</subject><subject>Gene Expression Regulation, Fungal</subject><subject>Genes</subject><subject>GOLGI APPARATUS</subject><subject>IMMUNOCYTOCHEMISTRY</subject><subject>IMMUNOLOGIE</subject><subject>IMMUNOLOGY</subject><subject>INMUNOLOGIA</subject><subject>MEMBRANAS CELULARES</subject><subject>MEMBRANE CELLULAIRE</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>MEMBRANE VESICLES</subject><subject>Membranes</subject><subject>METABOLISME DES PROTEINES</subject><subject>METABOLISMO PROTEICO</subject><subject>MOLECULAR SEQUENCE DATA</subject><subject>MUTANT</subject><subject>MUTANTES</subject><subject>MUTANTS</subject><subject>ORGANITE CELLULAIRE</subject><subject>ORGANULOS CITOPLASMICOS</subject><subject>PEPTIDASAS</subject><subject>PEPTIDASE</subject><subject>PEPTIDASES</subject><subject>Plasmids</subject><subject>PROTEIN METABOLISM</subject><subject>PROTEIN TRANSPORT</subject><subject>PROTEINAS</subject><subject>PROTEINAS AGLUTINANTES</subject><subject>PROTEINE</subject><subject>PROTEINE DE LIAISON</subject><subject>PROTEINS</subject><subject>Qa-SNARE Proteins</subject><subject>Qb-SNARE Proteins</subject><subject>REGULATION</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>SECRECION</subject><subject>SECRETION</subject><subject>Traffic</subject><subject>Transport vesicles</subject><subject>VACUOLA</subject><subject>VACUOLE</subject><subject>VACUOLES</subject><subject>Vesicular Transport Proteins</subject><subject>Yeast</subject><subject>Yeasts</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1vEzEQxVcIVELhygkkiwO3XTz-WK8vSFVVClIFiLRcLa_jzTpK1lvbmyj_fR0lKoULJx_e7z3PzCuKt4ArwA39tDJtBVRUogIO8KyYAWe4bIDh58UMYwKl5IS_LF7FuMIYM8HoWXEmQUqoxazY3fYW7a2OCW3L-feLX1fod3Iwoo1dOJ1sRGnn0dZGZ9YWpaCHOPqQ0KhTv9P7LPfBT8seuSHZoE1yfoho51KflWw4ZkY0tws-Ij0s0E87AhlfFy86vY72zek9L-6-XN1efi1vflx_u7y4KQ1r6lQCbThjrOvAMCA10QQb2mAuoSN6YUGatml1gzMlsJYt7aClzEjLDTVGcnpefD7mjlObVzJ2yDus1RjcRoe98tqpv5XB9Wrpt4rkozbkEPDxFBD8_WRjUhsXjV2v9WD9FJWQuGEM6H9BqAFzXtcZ_PAPuPJTGPIV8qcCC1JzmaHqCJngYwy2exwZsDoUr3LxKs-ohDoUnw3vny76iJ-azvq7o76KyYc_aTU0gJ_YO-2VXgYX1d08WwXmtJY1fQAUDLtv</recordid><startdate>19970630</startdate><enddate>19970630</enddate><creator>Von Mollard, G.F. (University of Oregon, Eugene, OR.)</creator><creator>Nothwehr, S.F</creator><creator>Stevens, T.H</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</general><scope>FBQ</scope><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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19970630</creationdate><title>The yeast v-SNARE Vti1p mediates two vesicle transport pathways through interactions with the t-SNAREs Sed5p and Pep12p</title><author>Von Mollard, G.F. (University of Oregon, Eugene, OR.) ; Nothwehr, S.F ; Stevens, T.H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c486t-1385444ff1c41262a20c380591f2ade19cb8ba8085470a9b3f1b34c9e5c3cc953</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>AMINO ACID SEQUENCES</topic><topic>Amino acids</topic><topic>APARATO GOLGI</topic><topic>APPAREIL DE GOLGI</topic><topic>BETA-FRUCTOFURANOSIDASE</topic><topic>BINDING PROTEINS</topic><topic>Biological transport</topic><topic>Biological Transport - genetics</topic><topic>CARBOXYPEPTIDASES</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell growth</topic><topic>CELL MEMBRANES</topic><topic>Cells</topic><topic>Cellular biology</topic><topic>CHEMICAL COMPOSITION</topic><topic>COMPOSICION QUIMICA</topic><topic>COMPOSITION CHIMIQUE</topic><topic>Cytoplasmic Granules - genetics</topic><topic>Cytoplasmic Granules - metabolism</topic><topic>CYTOPLASMIC ORGANELLES</topic><topic>FRUCTOFURANOSIDASA</topic><topic>FRUCTOFURANOSIDASE</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>GENBANK/AF00674</topic><topic>Gene Expression Regulation, Fungal</topic><topic>Genes</topic><topic>GOLGI APPARATUS</topic><topic>IMMUNOCYTOCHEMISTRY</topic><topic>IMMUNOLOGIE</topic><topic>IMMUNOLOGY</topic><topic>INMUNOLOGIA</topic><topic>MEMBRANAS CELULARES</topic><topic>MEMBRANE CELLULAIRE</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>MEMBRANE VESICLES</topic><topic>Membranes</topic><topic>METABOLISME DES PROTEINES</topic><topic>METABOLISMO PROTEICO</topic><topic>MOLECULAR SEQUENCE DATA</topic><topic>MUTANT</topic><topic>MUTANTES</topic><topic>MUTANTS</topic><topic>ORGANITE CELLULAIRE</topic><topic>ORGANULOS CITOPLASMICOS</topic><topic>PEPTIDASAS</topic><topic>PEPTIDASE</topic><topic>PEPTIDASES</topic><topic>Plasmids</topic><topic>PROTEIN METABOLISM</topic><topic>PROTEIN TRANSPORT</topic><topic>PROTEINAS</topic><topic>PROTEINAS AGLUTINANTES</topic><topic>PROTEINE</topic><topic>PROTEINE DE LIAISON</topic><topic>PROTEINS</topic><topic>Qa-SNARE Proteins</topic><topic>Qb-SNARE Proteins</topic><topic>REGULATION</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>SECRECION</topic><topic>SECRETION</topic><topic>Traffic</topic><topic>Transport vesicles</topic><topic>VACUOLA</topic><topic>VACUOLE</topic><topic>VACUOLES</topic><topic>Vesicular Transport Proteins</topic><topic>Yeast</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Von Mollard, G.F. (University of Oregon, Eugene, OR.)</creatorcontrib><creatorcontrib>Nothwehr, S.F</creatorcontrib><creatorcontrib>Stevens, T.H</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Von Mollard, G.F. (University of Oregon, Eugene, OR.)</au><au>Nothwehr, S.F</au><au>Stevens, T.H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The yeast v-SNARE Vti1p mediates two vesicle transport pathways through interactions with the t-SNAREs Sed5p and Pep12p</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>1997-06-30</date><risdate>1997</risdate><volume>137</volume><issue>7</issue><spage>1511</spage><epage>1524</epage><pages>1511-1524</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>Membrane traffic in eukaryotic cells requires that specific v-SNAREs on transport vesicles interact with specific t-SNAREs on target membranes. We identified a novel Saccharomyces cerevisiae v-SNARE (Vti1p) encoded by the essential gene, VTI1. Vti1p interacts with the prevacuolar t-SNARE Pep12p to direct Golgi to prevacuolar traffic. vti1-1 mutant cells missorted and secreted the soluble vacuolar hydrolase carboxypeptidase Y (CPY) rapidly and reversibly when vti1-1 cells were shifted to the restrictive temperature. However, overexpression of Pep12p suppressed the CPY secretion defect exhibited by vti1-1 cells at 36 degrees C. Characterization of a second vti1 mutant, vti1-11, revealed that Vti1p also plays a role in membrane traffic at a cis-Golgi stage. vti1 -11 mutant cells displayed a growth defect and accumulated the ER and early Golgi forms of both CPY and the secreted protein invertase at the nonpermissive temperature. Overexpression of the yeast cis-Golgi t-SNARE Sed5p suppressed the accumulation of the ER form of CPY but did not lead to CPY transport to the vacuole in vti1-11 cells. Overexpression of Sed5p allowed growth in the absence of Vti1p. In vitro binding and coimmunoprecipitation studies revealed that Vti1p interacts directly with the two t-SNAREs, Sed5p and Pep12p. These data suggest that Vti1p plays a role in cis-Golgi membrane traffic, which is essential for yeast viability, and a nonessential role in the fusion of Golgi-derived vesicles with the prevacuolar compartment. Therefore, a single v-SNARE can interact functionally with two different t-SNAREs in directing membrane traffic in yeast</abstract><cop>United States</cop><pub>Rockefeller University Press</pub><pmid>9199167</pmid><doi>10.1083/jcb.137.7.1511</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9525 |
| ispartof | The Journal of cell biology, 1997-06, Vol.137 (7), p.1511-1524 |
| issn | 0021-9525 1540-8140 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2137825 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | AMINO ACID SEQUENCES Amino acids APARATO GOLGI APPAREIL DE GOLGI BETA-FRUCTOFURANOSIDASE BINDING PROTEINS Biological transport Biological Transport - genetics CARBOXYPEPTIDASES Carrier Proteins - genetics Carrier Proteins - metabolism Cell growth CELL MEMBRANES Cells Cellular biology CHEMICAL COMPOSITION COMPOSICION QUIMICA COMPOSITION CHIMIQUE Cytoplasmic Granules - genetics Cytoplasmic Granules - metabolism CYTOPLASMIC ORGANELLES FRUCTOFURANOSIDASA FRUCTOFURANOSIDASE Fungal Proteins - genetics Fungal Proteins - metabolism GENBANK/AF00674 Gene Expression Regulation, Fungal Genes GOLGI APPARATUS IMMUNOCYTOCHEMISTRY IMMUNOLOGIE IMMUNOLOGY INMUNOLOGIA MEMBRANAS CELULARES MEMBRANE CELLULAIRE Membrane Proteins - genetics Membrane Proteins - metabolism MEMBRANE VESICLES Membranes METABOLISME DES PROTEINES METABOLISMO PROTEICO MOLECULAR SEQUENCE DATA MUTANT MUTANTES MUTANTS ORGANITE CELLULAIRE ORGANULOS CITOPLASMICOS PEPTIDASAS PEPTIDASE PEPTIDASES Plasmids PROTEIN METABOLISM PROTEIN TRANSPORT PROTEINAS PROTEINAS AGLUTINANTES PROTEINE PROTEINE DE LIAISON PROTEINS Qa-SNARE Proteins Qb-SNARE Proteins REGULATION SACCHAROMYCES CEREVISIAE Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae - ultrastructure Saccharomyces cerevisiae Proteins SECRECION SECRETION Traffic Transport vesicles VACUOLA VACUOLE VACUOLES Vesicular Transport Proteins Yeast Yeasts |
| title | The yeast v-SNARE Vti1p mediates two vesicle transport pathways through interactions with the t-SNAREs Sed5p and Pep12p |
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