Membrane transport in Caenorhabditis elegans: an essential role for VPS34 at the nuclear membrane
Here we present a detailed genetic analysis of let‐512/vps34 that encodes the Caenorhabditis elegans homologue of the yeast phosphatidylinositol 3‐kinase Vps34p. LET‐512/VPS34 has essential functions and is ubiquitously expressed in all tissues and developmental stages. It accumulates at a perinucle...
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| Veröffentlicht in: | The EMBO journal 2002-04, Vol.21 (7), p.1673-1683 |
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| creator | Roggo, Lorenz Bernard, Vincent Kovacs, Attila L. Rose, Ann M. Savoy, Fabienne Zetka, Monique Wymann, Matthias P. Müller, Fritz |
| description | Here we present a detailed genetic analysis of
let‐512/vps34
that encodes the
Caenorhabditis elegans
homologue of the yeast phosphatidylinositol 3‐kinase Vps34p. LET‐512/VPS34 has essential functions and is ubiquitously expressed in all tissues and developmental stages. It accumulates at a perinuclear region, and mutations in
let‐512/vps34
result in an expansion of the outer nuclear membrane as well as in a mislocalization and subsequent complete lack of expression of LRP‐1, a
C.elegans
LDL receptor normally associated with the apical surface of hypodermal cells. Using a GFP::2xFYVE fusion protein we found that the phosphatidylinositol 3‐phosphate (PtdIns 3‐P) product of LET‐512/VPS34 is associated with a multitude of intracellular membranes and vesicles located at the periphery, including endocytic vesicles. We propose that LET‐512/VPS34 is required for membrane transport from the outer nuclear membrane towards the cell periphery. Thus, LET‐512/VPS34 may regulate the secretory pathway in a much broader range of compartments than was previously suggested for the yeast orthologue. |
| doi_str_mv | 10.1093/emboj/21.7.1673 |
| format | Article |
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let‐512/vps34
that encodes the
Caenorhabditis elegans
homologue of the yeast phosphatidylinositol 3‐kinase Vps34p. LET‐512/VPS34 has essential functions and is ubiquitously expressed in all tissues and developmental stages. It accumulates at a perinuclear region, and mutations in
let‐512/vps34
result in an expansion of the outer nuclear membrane as well as in a mislocalization and subsequent complete lack of expression of LRP‐1, a
C.elegans
LDL receptor normally associated with the apical surface of hypodermal cells. Using a GFP::2xFYVE fusion protein we found that the phosphatidylinositol 3‐phosphate (PtdIns 3‐P) product of LET‐512/VPS34 is associated with a multitude of intracellular membranes and vesicles located at the periphery, including endocytic vesicles. We propose that LET‐512/VPS34 is required for membrane transport from the outer nuclear membrane towards the cell periphery. Thus, LET‐512/VPS34 may regulate the secretory pathway in a much broader range of compartments than was previously suggested for the yeast orthologue.</description><identifier>ISSN: 0261-4189</identifier><identifier>ISSN: 1460-2075</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1093/emboj/21.7.1673</identifier><identifier>PMID: 11927551</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Amino Acid Sequence ; Animals ; Biological Transport ; Caenorhabditis elegans ; Caenorhabditis elegans - enzymology ; Caenorhabditis elegans - genetics ; Caenorhabditis elegans Proteins - genetics ; Caenorhabditis elegans Proteins - metabolism ; Cell Nucleus - metabolism ; Developmental stages ; EMBO20 ; Endocytosis - physiology ; Gene Expression ; membrane transport ; Membranes ; Molecular Sequence Data ; Mutagenesis ; Nuclear Envelope - metabolism ; Phosphatidylinositol 3-Kinases - genetics ; Phosphatidylinositol 3-Kinases - metabolism ; PtdIns 3-kinase ; Transport Vesicles - metabolism ; Yeasts</subject><ispartof>The EMBO journal, 2002-04, Vol.21 (7), p.1673-1683</ispartof><rights>European Molecular Biology Organization 2002</rights><rights>Copyright © 2002 European Molecular Biology Organization</rights><rights>Copyright Oxford University Press(England) Apr 01, 2002</rights><rights>Copyright © 2002 European Molecular Biology Organization 2002</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6316-df4fc3ff82d80433dc36f98a9f9b4ddf7ac4b0382478a743564e4a15b7a82e723</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/PMC125367/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC125367/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,315,728,781,785,886,1418,1434,27926,27927,45576,45577,46411,46835,53793,53795</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11927551$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Roggo, Lorenz</creatorcontrib><creatorcontrib>Bernard, Vincent</creatorcontrib><creatorcontrib>Kovacs, Attila L.</creatorcontrib><creatorcontrib>Rose, Ann M.</creatorcontrib><creatorcontrib>Savoy, Fabienne</creatorcontrib><creatorcontrib>Zetka, Monique</creatorcontrib><creatorcontrib>Wymann, Matthias P.</creatorcontrib><creatorcontrib>Müller, Fritz</creatorcontrib><title>Membrane transport in Caenorhabditis elegans: an essential role for VPS34 at the nuclear membrane</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>Here we present a detailed genetic analysis of
let‐512/vps34
that encodes the
Caenorhabditis elegans
homologue of the yeast phosphatidylinositol 3‐kinase Vps34p. LET‐512/VPS34 has essential functions and is ubiquitously expressed in all tissues and developmental stages. It accumulates at a perinuclear region, and mutations in
let‐512/vps34
result in an expansion of the outer nuclear membrane as well as in a mislocalization and subsequent complete lack of expression of LRP‐1, a
C.elegans
LDL receptor normally associated with the apical surface of hypodermal cells. Using a GFP::2xFYVE fusion protein we found that the phosphatidylinositol 3‐phosphate (PtdIns 3‐P) product of LET‐512/VPS34 is associated with a multitude of intracellular membranes and vesicles located at the periphery, including endocytic vesicles. We propose that LET‐512/VPS34 is required for membrane transport from the outer nuclear membrane towards the cell periphery. Thus, LET‐512/VPS34 may regulate the secretory pathway in a much broader range of compartments than was previously suggested for the yeast orthologue.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Biological Transport</subject><subject>Caenorhabditis elegans</subject><subject>Caenorhabditis elegans - enzymology</subject><subject>Caenorhabditis elegans - genetics</subject><subject>Caenorhabditis elegans Proteins - genetics</subject><subject>Caenorhabditis elegans Proteins - metabolism</subject><subject>Cell Nucleus - metabolism</subject><subject>Developmental stages</subject><subject>EMBO20</subject><subject>Endocytosis - physiology</subject><subject>Gene Expression</subject><subject>membrane transport</subject><subject>Membranes</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis</subject><subject>Nuclear Envelope - metabolism</subject><subject>Phosphatidylinositol 3-Kinases - genetics</subject><subject>Phosphatidylinositol 3-Kinases - metabolism</subject><subject>PtdIns 3-kinase</subject><subject>Transport Vesicles - metabolism</subject><subject>Yeasts</subject><issn>0261-4189</issn><issn>1460-2075</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFUcuO0zAUtRCIKYU1K5DFgl1aP-MEiQUThgE0hZF4LS0nuWlTErvYCTB_j0uqzoCEkCV7cR73XB-EHlKyoCTnS-hLt10yulALmip-C82oSEnCiJK30YywlCaCZvkJuhfClhAiM0XvohNKc6akpDNkVtHCGwt4iHfYOT_g1uLCgHV-Y8q6HdqAoYN1RJ9hYzGEAHZoTYe96wA3zuPPlx-4wGbAwwawHasOjMf9wfg-utOYLsCDwztHn16dfSxeJxfvz98ULy6SKuU0TepGNBVvmozVGRGc1xVPmzwzeZOXoq4bZSpREp4xoTKjBJepAGGoLJXJGCjG5-j55Lsbyx7qKob0ptM73_bGX2lnWv0nYtuNXrvvmjLJ49_N0dOD3rtvI4RB922ooOviDm4MWlEpuVAkEp_8Rdy60du4m6a5ZPGIvdtyIlXeheChOQahRO-r07-r04xqpffVRcXjm_mv-YeuIiGbCD_aDq7-56fPVqdvlcwFz9IoJZM0RJVdg78R-Z9xHk0Sa4bRw3HctWUy4W0Y4OcRNv6rjnIl9Zd35zovxOXpy1WhGf8Fcv3Q-g</recordid><startdate>20020401</startdate><enddate>20020401</enddate><creator>Roggo, Lorenz</creator><creator>Bernard, Vincent</creator><creator>Kovacs, Attila L.</creator><creator>Rose, Ann M.</creator><creator>Savoy, Fabienne</creator><creator>Zetka, Monique</creator><creator>Wymann, Matthias P.</creator><creator>Müller, Fritz</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</general><general>Oxford University Press</general><scope>BSCLL</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>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20020401</creationdate><title>Membrane transport in Caenorhabditis elegans: an essential role for VPS34 at the nuclear membrane</title><author>Roggo, Lorenz ; Bernard, Vincent ; Kovacs, Attila L. ; Rose, Ann M. ; Savoy, Fabienne ; Zetka, Monique ; Wymann, Matthias P. ; Müller, Fritz</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6316-df4fc3ff82d80433dc36f98a9f9b4ddf7ac4b0382478a743564e4a15b7a82e723</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Biological Transport</topic><topic>Caenorhabditis elegans</topic><topic>Caenorhabditis elegans - enzymology</topic><topic>Caenorhabditis elegans - genetics</topic><topic>Caenorhabditis elegans Proteins - genetics</topic><topic>Caenorhabditis elegans Proteins - metabolism</topic><topic>Cell Nucleus - metabolism</topic><topic>Developmental stages</topic><topic>EMBO20</topic><topic>Endocytosis - physiology</topic><topic>Gene Expression</topic><topic>membrane transport</topic><topic>Membranes</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis</topic><topic>Nuclear Envelope - metabolism</topic><topic>Phosphatidylinositol 3-Kinases - genetics</topic><topic>Phosphatidylinositol 3-Kinases - metabolism</topic><topic>PtdIns 3-kinase</topic><topic>Transport Vesicles - metabolism</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Roggo, Lorenz</creatorcontrib><creatorcontrib>Bernard, Vincent</creatorcontrib><creatorcontrib>Kovacs, Attila L.</creatorcontrib><creatorcontrib>Rose, Ann M.</creatorcontrib><creatorcontrib>Savoy, Fabienne</creatorcontrib><creatorcontrib>Zetka, Monique</creatorcontrib><creatorcontrib>Wymann, Matthias P.</creatorcontrib><creatorcontrib>Müller, Fritz</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</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>Roggo, Lorenz</au><au>Bernard, Vincent</au><au>Kovacs, Attila L.</au><au>Rose, Ann M.</au><au>Savoy, Fabienne</au><au>Zetka, Monique</au><au>Wymann, Matthias P.</au><au>Müller, Fritz</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Membrane transport in Caenorhabditis elegans: an essential role for VPS34 at the nuclear membrane</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2002-04-01</date><risdate>2002</risdate><volume>21</volume><issue>7</issue><spage>1673</spage><epage>1683</epage><pages>1673-1683</pages><issn>0261-4189</issn><issn>1460-2075</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>Here we present a detailed genetic analysis of
let‐512/vps34
that encodes the
Caenorhabditis elegans
homologue of the yeast phosphatidylinositol 3‐kinase Vps34p. LET‐512/VPS34 has essential functions and is ubiquitously expressed in all tissues and developmental stages. It accumulates at a perinuclear region, and mutations in
let‐512/vps34
result in an expansion of the outer nuclear membrane as well as in a mislocalization and subsequent complete lack of expression of LRP‐1, a
C.elegans
LDL receptor normally associated with the apical surface of hypodermal cells. Using a GFP::2xFYVE fusion protein we found that the phosphatidylinositol 3‐phosphate (PtdIns 3‐P) product of LET‐512/VPS34 is associated with a multitude of intracellular membranes and vesicles located at the periphery, including endocytic vesicles. We propose that LET‐512/VPS34 is required for membrane transport from the outer nuclear membrane towards the cell periphery. Thus, LET‐512/VPS34 may regulate the secretory pathway in a much broader range of compartments than was previously suggested for the yeast orthologue.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>11927551</pmid><doi>10.1093/emboj/21.7.1673</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Animals Biological Transport Caenorhabditis elegans Caenorhabditis elegans - enzymology Caenorhabditis elegans - genetics Caenorhabditis elegans Proteins - genetics Caenorhabditis elegans Proteins - metabolism Cell Nucleus - metabolism Developmental stages EMBO20 Endocytosis - physiology Gene Expression membrane transport Membranes Molecular Sequence Data Mutagenesis Nuclear Envelope - metabolism Phosphatidylinositol 3-Kinases - genetics Phosphatidylinositol 3-Kinases - metabolism PtdIns 3-kinase Transport Vesicles - metabolism Yeasts |
| title | Membrane transport in Caenorhabditis elegans: an essential role for VPS34 at the nuclear membrane |
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