Vps33B is required for delivery of endocytosed cargo to lysosomes.
Identifieur interne : 002550 ( PubMed/Curation ); précédent : 002549; suivant : 002551Vps33B is required for delivery of endocytosed cargo to lysosomes.
Auteurs : Romain Galmes [Pays-Bas] ; Corlinda Ten Brink [Pays-Bas] ; Viola Oorschot [Pays-Bas] ; Tineke Veenendaal [Pays-Bas] ; Caspar Jonker [Pays-Bas] ; Peter Van Der Sluijs [Pays-Bas] ; Judith Klumperman [Pays-Bas]Source :
- Traffic (Copenhagen, Denmark) [ 1600-0854 ] ; 2015.
Descripteurs français
- KwdFr :
- Cellules HeLa, Endocytose (physiologie), Endosomes (métabolisme), Endosomes (ultrastructure), Fusion membranaire (physiologie), Humains, Lysosomes (métabolisme), Lysosomes (ultrastructure), Microscopie de fluorescence, Microscopie électronique, Protéines du transport vésiculaire (), Protéines du transport vésiculaire (génétique), Protéines du transport vésiculaire (métabolisme), Techniques de knock-down de gènes, Transport de protéines.
- MESH :
- génétique : Protéines du transport vésiculaire.
- métabolisme : Endosomes, Lysosomes, Protéines du transport vésiculaire.
- physiologie : Endocytose, Fusion membranaire.
- Cellules HeLa, Endosomes, Humains, Lysosomes, Microscopie de fluorescence, Microscopie électronique, Protéines du transport vésiculaire, Techniques de knock-down de gènes, Transport de protéines.
English descriptors
- KwdEn :
- Endocytosis (physiology), Endosomes (metabolism), Endosomes (ultrastructure), Gene Knockdown Techniques, HeLa Cells, Humans, Lysosomes (metabolism), Lysosomes (ultrastructure), Membrane Fusion (physiology), Microscopy, Electron, Microscopy, Fluorescence, Protein Transport, Vesicular Transport Proteins (chemistry), Vesicular Transport Proteins (genetics), Vesicular Transport Proteins (metabolism).
- MESH :
- chemical , chemistry : Vesicular Transport Proteins.
- chemical , genetics : Vesicular Transport Proteins.
- metabolism : Endosomes, Lysosomes, Vesicular Transport Proteins.
- physiology : Endocytosis, Membrane Fusion.
- ultrastructure : Endosomes, Lysosomes.
- Gene Knockdown Techniques, HeLa Cells, Humans, Microscopy, Electron, Microscopy, Fluorescence, Protein Transport.
Abstract
Lysosomes are the main degradative compartments of eukaryotic cells. The CORVET and HOPS tethering complexes are well known for their role in membrane fusion in the yeast endocytic pathway. Yeast Vps33p is part of both complexes, and has two mammalian homologues: Vps33A and Vps33B. Vps33B is required for recycling of apical proteins in polarized cells and a causative gene for ARC syndrome. Here, we investigate whether Vps33B is also required in the degradative pathway. By fluorescence and electron microscopy we show that Vps33B depletion in HeLa cells leads to significantly increased numbers of late endosomes that together with lysosomes accumulate in the perinuclear region. Degradation of endocytosed cargo is impaired in these cells. By electron microscopy we show that endocytosed BSA-gold reaches late endosomes, but is decreased in lysosomes. The increase in late endosome numbers and the lack of internalized cargo in lysosomes are indicative for a defect in late endosomal-lysosomal fusion events, which explains the observed decrease in cargo degradation. A corresponding phenotype was found after Vps33A knock down, which in addition also resulted in decreased lysosome numbers. We conclude that Vps33B, in addition to its role in endosomal recycling, is required for late endosomal-lysosomal fusion events.
DOI: 10.1111/tra.12334
PubMed: 26403612
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Utrecht</wicri:regionArea></affiliation></author><author><name sortKey="Jonker, Caspar" sort="Jonker, Caspar" uniqKey="Jonker C" first="Caspar" last="Jonker">Caspar Jonker</name><affiliation wicri:level="1"><nlm:affiliation>Department of Cell Biology and Institute of Biomembranes, Center for Molecular Medicine, University Medical Center Utrecht, Heidelberglaan 100, 3584CX, Utrecht, The Netherlands.</nlm:affiliation><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Department of Cell Biology and Institute of Biomembranes, Center for Molecular Medicine, University Medical Center Utrecht, Heidelberglaan 100, 3584CX, Utrecht</wicri:regionArea></affiliation></author><author><name sortKey="Van Der Sluijs, Peter" sort="Van Der Sluijs, Peter" uniqKey="Van Der Sluijs P" first="Peter" last="Van Der Sluijs">Peter Van Der Sluijs</name><affiliation wicri:level="1"><nlm:affiliation>Department of Cell Biology and Institute of Biomembranes, Center for Molecular Medicine, University Medical 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(physiologie)</term><term>Endosomes (métabolisme)</term><term>Endosomes (ultrastructure)</term><term>Fusion membranaire (physiologie)</term><term>Humains</term><term>Lysosomes (métabolisme)</term><term>Lysosomes (ultrastructure)</term><term>Microscopie de fluorescence</term><term>Microscopie électronique</term><term>Protéines du transport vésiculaire ()</term><term>Protéines du transport vésiculaire (génétique)</term><term>Protéines du transport vésiculaire (métabolisme)</term><term>Techniques de knock-down de gènes</term><term>Transport de protéines</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Vesicular Transport Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Vesicular Transport Proteins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines du transport vésiculaire</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Endosomes</term><term>Lysosomes</term><term>Vesicular Transport Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Endosomes</term><term>Lysosomes</term><term>Protéines du transport vésiculaire</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Endocytose</term><term>Fusion membranaire</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Endocytosis</term><term>Membrane Fusion</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Endosomes</term><term>Lysosomes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Gene Knockdown Techniques</term><term>HeLa Cells</term><term>Humans</term><term>Microscopy, Electron</term><term>Microscopy, Fluorescence</term><term>Protein Transport</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cellules HeLa</term><term>Endosomes</term><term>Humains</term><term>Lysosomes</term><term>Microscopie de fluorescence</term><term>Microscopie électronique</term><term>Protéines du transport vésiculaire</term><term>Techniques de knock-down de gènes</term><term>Transport de protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Lysosomes are the main degradative compartments of eukaryotic cells. The CORVET and HOPS tethering complexes are well known for their role in membrane fusion in the yeast endocytic pathway. Yeast Vps33p is part of both complexes, and has two mammalian homologues: Vps33A and Vps33B. Vps33B is required for recycling of apical proteins in polarized cells and a causative gene for ARC syndrome. Here, we investigate whether Vps33B is also required in the degradative pathway. By fluorescence and electron microscopy we show that Vps33B depletion in HeLa cells leads to significantly increased numbers of late endosomes that together with lysosomes accumulate in the perinuclear region. Degradation of endocytosed cargo is impaired in these cells. By electron microscopy we show that endocytosed BSA-gold reaches late endosomes, but is decreased in lysosomes. The increase in late endosome numbers and the lack of internalized cargo in lysosomes are indicative for a defect in late endosomal-lysosomal fusion events, which explains the observed decrease in cargo degradation. A corresponding phenotype was found after Vps33A knock down, which in addition also resulted in decreased lysosome numbers. We conclude that Vps33B, in addition to its role in endosomal recycling, is required for late endosomal-lysosomal fusion events.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26403612</PMID><DateCreated><Year>2016</Year><Month>01</Month><Day>16</Day></DateCreated><DateCompleted><Year>2016</Year><Month>10</Month><Day>24</Day></DateCompleted><DateRevised><Year>2016</Year><Month>12</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1600-0854</ISSN><JournalIssue CitedMedium="Internet"><Volume>16</Volume><Issue>12</Issue><PubDate><Year>2015</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Traffic (Copenhagen, Denmark)</Title><ISOAbbreviation>Traffic</ISOAbbreviation></Journal><ArticleTitle>Vps33B is required for delivery of endocytosed cargo to lysosomes.</ArticleTitle><Pagination><MedlinePgn>1288-305</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1111/tra.12334</ELocationID><Abstract><AbstractText>Lysosomes are the main degradative compartments of eukaryotic cells. The CORVET and HOPS tethering complexes are well known for their role in membrane fusion in the yeast endocytic pathway. Yeast Vps33p is part of both complexes, and has two mammalian homologues: Vps33A and Vps33B. Vps33B is required for recycling of apical proteins in polarized cells and a causative gene for ARC syndrome. Here, we investigate whether Vps33B is also required in the degradative pathway. By fluorescence and electron microscopy we show that Vps33B depletion in HeLa cells leads to significantly increased numbers of late endosomes that together with lysosomes accumulate in the perinuclear region. Degradation of endocytosed cargo is impaired in these cells. By electron microscopy we show that endocytosed BSA-gold reaches late endosomes, but is decreased in lysosomes. The increase in late endosome numbers and the lack of internalized cargo in lysosomes are indicative for a defect in late endosomal-lysosomal fusion events, which explains the observed decrease in cargo degradation. A corresponding phenotype was found after Vps33A knock down, which in addition also resulted in decreased lysosome numbers. We conclude that Vps33B, in addition to its role in endosomal recycling, is required for late endosomal-lysosomal fusion events.</AbstractText><CopyrightInformation>© 2015 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Galmes</LastName><ForeName>Romain</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Department of Cell Biology and Institute of Biomembranes, Center for Molecular Medicine, University Medical Center Utrecht, Heidelberglaan 100, 3584CX, Utrecht, The Netherlands.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Present address: Institut Jacques Monod, CNRS, UMR7592, Université Paris Diderot, Sorbonne Paris Cité, F-75013, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>ten Brink</LastName><ForeName>Corlinda</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Department of Cell Biology and Institute of Biomembranes, Center for Molecular Medicine, University Medical Center Utrecht, Heidelberglaan 100, 3584CX, Utrecht, The Netherlands.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Oorschot</LastName><ForeName>Viola</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Department of Cell Biology and Institute of Biomembranes, Center for Molecular Medicine, University Medical Center Utrecht, Heidelberglaan 100, 3584CX, Utrecht, The Netherlands.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Present address: Monash Micro Imaging, 15 Innovation Walk, Strip 1 Monash Biotechnology, Monash University, Clayton, VIC, 3800, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Veenendaal</LastName><ForeName>Tineke</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Department of Cell Biology and Institute of Biomembranes, Center for Molecular Medicine, University Medical Center Utrecht, Heidelberglaan 100, 3584CX, Utrecht, The Netherlands.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jonker</LastName><ForeName>Caspar</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Department of Cell Biology and Institute of Biomembranes, Center for Molecular Medicine, University Medical Center Utrecht, Heidelberglaan 100, 3584CX, Utrecht, The Netherlands.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>van der Sluijs</LastName><ForeName>Peter</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Department of Cell Biology and Institute of Biomembranes, Center for Molecular Medicine, University Medical Center Utrecht, Heidelberglaan 100, 3584CX, Utrecht, The Netherlands.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Klumperman</LastName><ForeName>Judith</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Cell Biology and Institute of Biomembranes, Center for Molecular Medicine, University Medical Center Utrecht, Heidelberglaan 100, 3584CX, Utrecht, The Netherlands.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>10</Month><Day>21</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Traffic</MedlineTA><NlmUniqueID>100939340</NlmUniqueID><ISSNLinking>1398-9219</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C411584">VPS33B protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D033921">Vesicular Transport Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D004705" MajorTopicYN="N">Endocytosis</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011992" MajorTopicYN="N">Endosomes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D055785" MajorTopicYN="N">Gene Knockdown Techniques</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006367" MajorTopicYN="N">HeLa Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008247" MajorTopicYN="N">Lysosomes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008561" MajorTopicYN="N">Membrane Fusion</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008854" MajorTopicYN="N">Microscopy, Electron</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008856" MajorTopicYN="N">Microscopy, Fluorescence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D021381" MajorTopicYN="N">Protein Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D033921" MajorTopicYN="N">Vesicular Transport Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">HOPS complex</Keyword><Keyword MajorTopicYN="N">SM proteins</Keyword><Keyword MajorTopicYN="N">Vps33A</Keyword><Keyword MajorTopicYN="N">Vps33B</Keyword><Keyword MajorTopicYN="N">late endosomes</Keyword><Keyword MajorTopicYN="N">lysosomes</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>03</Month><Day>12</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2015</Year><Month>09</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>09</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>9</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>9</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>10</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26403612</ArticleId><ArticleId IdType="doi">10.1111/tra.12334</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour 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