Functionality and specific membrane localization of transport GTPases carrying C-terminal membrane anchors of synaptobrevin-like proteins
Ras-related guanine nucleotide-binding proteins of the Ypt/Rab family fulfill a pivotal role in vesicular protein transport both in yeast and in mammalian cells. Proper functioning of these proteins involves their cycling between a GTP- and a GDP-bound state as well as their reversible association w...
Gespeichert in:
| Veröffentlicht in: | The EMBO journal 1995-08, Vol.14 (15), p.3645-3653 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 3653 |
|---|---|
| container_issue | 15 |
| container_start_page | 3645 |
| container_title | The EMBO journal |
| container_volume | 14 |
| creator | Ossig, R Laufer, W Schmitt, H.D Gallwitz, D |
| description | Ras-related guanine nucleotide-binding proteins of the Ypt/Rab family fulfill a pivotal role in vesicular protein transport both in yeast and in mammalian cells. Proper functioning of these proteins involves their cycling between a GTP- and a GDP-bound state as well as their reversible association with specific membranes. Here we show that the yeast Ypt1 and Sec4 proteins, essential components of the vesicular transport machinery, allow unimpaired vesicular transport when permanently fixed to membranes by membrane-spanning domains replacing their two C-terminal cysteine residues. Membrane detachment of the GTPases therefore is not obligatory for transport vesicle docking to or fusion with an acceptor membrane. It was also found that the membrane anchors derived from different synaptobrevin-related proteins have targeting information and direct the chimeric GTPases to different cellular compartments, presumably from the endoplasmic reticulum via the secretory pathway. |
| doi_str_mv | 10.1002/j.1460-2075.1995.tb00034.x |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_394439</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>77451525</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5334-c5b7463232f7db0479be917e7166a14d2b0c45fc79656c67e11f7016a20e8cc03</originalsourceid><addsrcrecordid>eNqVkU1v0zAAhi3ENLrBT0BYHLgl2PFXjcRhVNtg2gQS29lyXKdzSexgp2PZP-Bf49CqgxPi4lh5P-RXDwCvMSoxQtXbdYkpR0WFBCuxlKwcaoQQoeX9EzDbS0_BDFUcFxTP5TNwlNI6m9hc4ENwKDjFfE5n4OfZxpvBBa9bN4xQ-yVMvTWucQZ2tquj9ha2wWT5QU8-GBo45L-pD3GA59dfdLIJGh3j6PwKLorBxs7luse49uY2xDQl0-h1P4Q62jvni9Z9s7CPYbDOp-fgoNFtsi9232Nwc3Z6vfhYXH4-_7Q4uSwMI4TmsxaUk4pUjVjWiApZW4mFFZhzjemyqpGhrDFCcsYNFxbjRiDMdYXs3BhEjsH7bW-_qTu7NNbnOa3qo-t0HFXQTv2teHerVuFOEUkpkTn_ZpeP4fvGpkF1Lhnbtnlq2CQlBGWYVeyfxgxA5h08G99tjSaGlKJt9o_BSE3A1VpNVNVEVU3A1Q64us_hl3_O2Ud3hLN-stV_uNaO_9GsTq8-XPy-545X245GB6VX0SV187VCmCDMkCRCkl-F38lJ</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>16893236</pqid></control><display><type>article</type><title>Functionality and specific membrane localization of transport GTPases carrying C-terminal membrane anchors of synaptobrevin-like proteins</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>Ossig, R ; Laufer, W ; Schmitt, H.D ; Gallwitz, D</creator><creatorcontrib>Ossig, R ; Laufer, W ; Schmitt, H.D ; Gallwitz, D</creatorcontrib><description>Ras-related guanine nucleotide-binding proteins of the Ypt/Rab family fulfill a pivotal role in vesicular protein transport both in yeast and in mammalian cells. Proper functioning of these proteins involves their cycling between a GTP- and a GDP-bound state as well as their reversible association with specific membranes. Here we show that the yeast Ypt1 and Sec4 proteins, essential components of the vesicular transport machinery, allow unimpaired vesicular transport when permanently fixed to membranes by membrane-spanning domains replacing their two C-terminal cysteine residues. Membrane detachment of the GTPases therefore is not obligatory for transport vesicle docking to or fusion with an acceptor membrane. It was also found that the membrane anchors derived from different synaptobrevin-related proteins have targeting information and direct the chimeric GTPases to different cellular compartments, presumably from the endoplasmic reticulum via the secretory pathway.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1002/j.1460-2075.1995.tb00034.x</identifier><identifier>PMID: 7641684</identifier><language>eng</language><publisher>England</publisher><subject>Amino Acid Sequence ; amino acid sequences ; beta-Fructofuranosidase ; binding proteins ; Biological Transport ; Cell Membrane - metabolism ; cell membranes ; cytochemistry ; Endoplasmic Reticulum - metabolism ; Fungal Proteins - chemistry ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; Glycoside Hydrolases - metabolism ; Glycosylation ; Golgi Apparatus - metabolism ; GTP Phosphohydrolases - chemistry ; GTP Phosphohydrolases - genetics ; GTP Phosphohydrolases - metabolism ; GTP-Binding Proteins - chemistry ; GTP-Binding Proteins - genetics ; GTP-Binding Proteins - metabolism ; guanine nucleotides ; guanosine diphosphate ; guanosine triphosphate ; guanosinetriphosphatase ; Membrane Proteins - chemistry ; membrane vesicles ; Molecular Sequence Data ; mutants ; Nerve Tissue Proteins - chemistry ; nucleotides ; organelles ; protein transport ; pyrophosphatases ; R-SNARE Proteins ; rab GTP-Binding Proteins ; Recombinant Fusion Proteins - metabolism ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins ; sec4 protein ; ypt1 proteins</subject><ispartof>The EMBO journal, 1995-08, Vol.14 (15), p.3645-3653</ispartof><rights>1995 European Molecular Biology Organization</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5334-c5b7463232f7db0479be917e7166a14d2b0c45fc79656c67e11f7016a20e8cc03</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC394439/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC394439/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,724,777,781,882,27905,27906,53772,53774</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7641684$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ossig, R</creatorcontrib><creatorcontrib>Laufer, W</creatorcontrib><creatorcontrib>Schmitt, H.D</creatorcontrib><creatorcontrib>Gallwitz, D</creatorcontrib><title>Functionality and specific membrane localization of transport GTPases carrying C-terminal membrane anchors of synaptobrevin-like proteins</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><description>Ras-related guanine nucleotide-binding proteins of the Ypt/Rab family fulfill a pivotal role in vesicular protein transport both in yeast and in mammalian cells. Proper functioning of these proteins involves their cycling between a GTP- and a GDP-bound state as well as their reversible association with specific membranes. Here we show that the yeast Ypt1 and Sec4 proteins, essential components of the vesicular transport machinery, allow unimpaired vesicular transport when permanently fixed to membranes by membrane-spanning domains replacing their two C-terminal cysteine residues. Membrane detachment of the GTPases therefore is not obligatory for transport vesicle docking to or fusion with an acceptor membrane. It was also found that the membrane anchors derived from different synaptobrevin-related proteins have targeting information and direct the chimeric GTPases to different cellular compartments, presumably from the endoplasmic reticulum via the secretory pathway.</description><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>beta-Fructofuranosidase</subject><subject>binding proteins</subject><subject>Biological Transport</subject><subject>Cell Membrane - metabolism</subject><subject>cell membranes</subject><subject>cytochemistry</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Fungal Proteins - chemistry</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>Glycoside Hydrolases - metabolism</subject><subject>Glycosylation</subject><subject>Golgi Apparatus - metabolism</subject><subject>GTP Phosphohydrolases - chemistry</subject><subject>GTP Phosphohydrolases - genetics</subject><subject>GTP Phosphohydrolases - metabolism</subject><subject>GTP-Binding Proteins - chemistry</subject><subject>GTP-Binding Proteins - genetics</subject><subject>GTP-Binding Proteins - metabolism</subject><subject>guanine nucleotides</subject><subject>guanosine diphosphate</subject><subject>guanosine triphosphate</subject><subject>guanosinetriphosphatase</subject><subject>Membrane Proteins - chemistry</subject><subject>membrane vesicles</subject><subject>Molecular Sequence Data</subject><subject>mutants</subject><subject>Nerve Tissue Proteins - chemistry</subject><subject>nucleotides</subject><subject>organelles</subject><subject>protein transport</subject><subject>pyrophosphatases</subject><subject>R-SNARE Proteins</subject><subject>rab GTP-Binding Proteins</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>sec4 protein</subject><subject>ypt1 proteins</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkU1v0zAAhi3ENLrBT0BYHLgl2PFXjcRhVNtg2gQS29lyXKdzSexgp2PZP-Bf49CqgxPi4lh5P-RXDwCvMSoxQtXbdYkpR0WFBCuxlKwcaoQQoeX9EzDbS0_BDFUcFxTP5TNwlNI6m9hc4ENwKDjFfE5n4OfZxpvBBa9bN4xQ-yVMvTWucQZ2tquj9ha2wWT5QU8-GBo45L-pD3GA59dfdLIJGh3j6PwKLorBxs7luse49uY2xDQl0-h1P4Q62jvni9Z9s7CPYbDOp-fgoNFtsi9232Nwc3Z6vfhYXH4-_7Q4uSwMI4TmsxaUk4pUjVjWiApZW4mFFZhzjemyqpGhrDFCcsYNFxbjRiDMdYXs3BhEjsH7bW-_qTu7NNbnOa3qo-t0HFXQTv2teHerVuFOEUkpkTn_ZpeP4fvGpkF1Lhnbtnlq2CQlBGWYVeyfxgxA5h08G99tjSaGlKJt9o_BSE3A1VpNVNVEVU3A1Q64us_hl3_O2Ud3hLN-stV_uNaO_9GsTq8-XPy-545X245GB6VX0SV187VCmCDMkCRCkl-F38lJ</recordid><startdate>199508</startdate><enddate>199508</enddate><creator>Ossig, R</creator><creator>Laufer, W</creator><creator>Schmitt, H.D</creator><creator>Gallwitz, D</creator><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>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>H94</scope><scope>M7N</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>199508</creationdate><title>Functionality and specific membrane localization of transport GTPases carrying C-terminal membrane anchors of synaptobrevin-like proteins</title><author>Ossig, R ; Laufer, W ; Schmitt, H.D ; Gallwitz, D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5334-c5b7463232f7db0479be917e7166a14d2b0c45fc79656c67e11f7016a20e8cc03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Amino Acid Sequence</topic><topic>amino acid sequences</topic><topic>beta-Fructofuranosidase</topic><topic>binding proteins</topic><topic>Biological Transport</topic><topic>Cell Membrane - metabolism</topic><topic>cell membranes</topic><topic>cytochemistry</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Fungal Proteins - chemistry</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>Glycoside Hydrolases - metabolism</topic><topic>Glycosylation</topic><topic>Golgi Apparatus - metabolism</topic><topic>GTP Phosphohydrolases - chemistry</topic><topic>GTP Phosphohydrolases - genetics</topic><topic>GTP Phosphohydrolases - metabolism</topic><topic>GTP-Binding Proteins - chemistry</topic><topic>GTP-Binding Proteins - genetics</topic><topic>GTP-Binding Proteins - metabolism</topic><topic>guanine nucleotides</topic><topic>guanosine diphosphate</topic><topic>guanosine triphosphate</topic><topic>guanosinetriphosphatase</topic><topic>Membrane Proteins - chemistry</topic><topic>membrane vesicles</topic><topic>Molecular Sequence Data</topic><topic>mutants</topic><topic>Nerve Tissue Proteins - chemistry</topic><topic>nucleotides</topic><topic>organelles</topic><topic>protein transport</topic><topic>pyrophosphatases</topic><topic>R-SNARE Proteins</topic><topic>rab GTP-Binding Proteins</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>sec4 protein</topic><topic>ypt1 proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ossig, R</creatorcontrib><creatorcontrib>Laufer, W</creatorcontrib><creatorcontrib>Schmitt, H.D</creatorcontrib><creatorcontrib>Gallwitz, D</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>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ossig, R</au><au>Laufer, W</au><au>Schmitt, H.D</au><au>Gallwitz, D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functionality and specific membrane localization of transport GTPases carrying C-terminal membrane anchors of synaptobrevin-like proteins</atitle><jtitle>The EMBO journal</jtitle><addtitle>EMBO J</addtitle><date>1995-08</date><risdate>1995</risdate><volume>14</volume><issue>15</issue><spage>3645</spage><epage>3653</epage><pages>3645-3653</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><abstract>Ras-related guanine nucleotide-binding proteins of the Ypt/Rab family fulfill a pivotal role in vesicular protein transport both in yeast and in mammalian cells. Proper functioning of these proteins involves their cycling between a GTP- and a GDP-bound state as well as their reversible association with specific membranes. Here we show that the yeast Ypt1 and Sec4 proteins, essential components of the vesicular transport machinery, allow unimpaired vesicular transport when permanently fixed to membranes by membrane-spanning domains replacing their two C-terminal cysteine residues. Membrane detachment of the GTPases therefore is not obligatory for transport vesicle docking to or fusion with an acceptor membrane. It was also found that the membrane anchors derived from different synaptobrevin-related proteins have targeting information and direct the chimeric GTPases to different cellular compartments, presumably from the endoplasmic reticulum via the secretory pathway.</abstract><cop>England</cop><pmid>7641684</pmid><doi>10.1002/j.1460-2075.1995.tb00034.x</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0261-4189 |
| ispartof | The EMBO journal, 1995-08, Vol.14 (15), p.3645-3653 |
| issn | 0261-4189 1460-2075 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_394439 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence amino acid sequences beta-Fructofuranosidase binding proteins Biological Transport Cell Membrane - metabolism cell membranes cytochemistry Endoplasmic Reticulum - metabolism Fungal Proteins - chemistry Fungal Proteins - genetics Fungal Proteins - metabolism Glycoside Hydrolases - metabolism Glycosylation Golgi Apparatus - metabolism GTP Phosphohydrolases - chemistry GTP Phosphohydrolases - genetics GTP Phosphohydrolases - metabolism GTP-Binding Proteins - chemistry GTP-Binding Proteins - genetics GTP-Binding Proteins - metabolism guanine nucleotides guanosine diphosphate guanosine triphosphate guanosinetriphosphatase Membrane Proteins - chemistry membrane vesicles Molecular Sequence Data mutants Nerve Tissue Proteins - chemistry nucleotides organelles protein transport pyrophosphatases R-SNARE Proteins rab GTP-Binding Proteins Recombinant Fusion Proteins - metabolism Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins sec4 protein ypt1 proteins |
| title | Functionality and specific membrane localization of transport GTPases carrying C-terminal membrane anchors of synaptobrevin-like proteins |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-19T12%3A30%3A17IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Functionality%20and%20specific%20membrane%20localization%20of%20transport%20GTPases%20carrying%20C-terminal%20membrane%20anchors%20of%20synaptobrevin-like%20proteins&rft.jtitle=The%20EMBO%20journal&rft.au=Ossig,%20R&rft.date=1995-08&rft.volume=14&rft.issue=15&rft.spage=3645&rft.epage=3653&rft.pages=3645-3653&rft.issn=0261-4189&rft.eissn=1460-2075&rft_id=info:doi/10.1002/j.1460-2075.1995.tb00034.x&rft_dat=%3Cproquest_pubme%3E77451525%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=16893236&rft_id=info:pmid/7641684&rfr_iscdi=true |