Rab4 and Rab7 Define Distinct Nonoverlapping Endosomal Compartments
Several Rab GTPases have been localized to distinct compartments of the endocytic pathway. Rab4 is associated with early endosomes and recycling vesicles and regulates membrane recycling from early endosomes. Rab7 is localized to late endosomes and is involved in the regulation of membrane transport...
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| Veröffentlicht in: | The Journal of biological chemistry 1996-11, Vol.271 (46), p.29191-29197 |
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| container_end_page | 29197 |
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| container_issue | 46 |
| container_start_page | 29191 |
| container_title | The Journal of biological chemistry |
| container_volume | 271 |
| creator | Bottger, G Nagelkerken, B van der Sluijs, P |
| description | Several Rab GTPases have been localized to distinct compartments of the endocytic pathway. Rab4 is associated with early endosomes
and recycling vesicles and regulates membrane recycling from early endosomes. Rab7 is localized to late endosomes and is involved
in the regulation of membrane transport between late endosomes and lysosomes. Although Rab4 and Rab7 appear to regulate distinct
transport events in endocytosis, it is not clear whether they perform their activities in related or entirely distinct intracellular
compartments. To address this question, we generated stable cell lines expressing Rab4 tagged with a novel X31 influenza hemagglutinin
(NH) epitope tag. These antibodies are characterized in this paper and were used to immunoisolate endocytic vesicles with
cytoplasmically exposed NHRab4. Immunoisolated membranes contain internalized 125 I-transferrin, but are devoid of Rab7. Confocal immunofluorescence microscopy showed that the early endosomal GTPases Rab4
and Rab5 both do not codistribute with Rab7 within the same cell. These observations suggest that each of the three Rab GTPases
operationally defines a distinct station of the endocytic pathway. |
| doi_str_mv | 10.1074/jbc.271.46.29191 |
| format | Article |
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and recycling vesicles and regulates membrane recycling from early endosomes. Rab7 is localized to late endosomes and is involved
in the regulation of membrane transport between late endosomes and lysosomes. Although Rab4 and Rab7 appear to regulate distinct
transport events in endocytosis, it is not clear whether they perform their activities in related or entirely distinct intracellular
compartments. To address this question, we generated stable cell lines expressing Rab4 tagged with a novel X31 influenza hemagglutinin
(NH) epitope tag. These antibodies are characterized in this paper and were used to immunoisolate endocytic vesicles with
cytoplasmically exposed NHRab4. Immunoisolated membranes contain internalized 125 I-transferrin, but are devoid of Rab7. Confocal immunofluorescence microscopy showed that the early endosomal GTPases Rab4
and Rab5 both do not codistribute with Rab7 within the same cell. These observations suggest that each of the three Rab GTPases
operationally defines a distinct station of the endocytic pathway.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.271.46.29191</identifier><identifier>PMID: 8910576</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Animals ; Cell Compartmentation ; CHO Cells ; Cricetinae ; Dogs ; Endocytosis ; Endosomes - metabolism ; GTP-Binding Proteins - metabolism ; HeLa Cells ; Humans ; Iodine Radioisotopes ; Microscopy, Confocal ; Microscopy, Fluorescence ; Molecular Sequence Data ; rab GTP-Binding Proteins ; rab4 GTP-Binding Proteins ; Transfection ; Transferrin - metabolism</subject><ispartof>The Journal of biological chemistry, 1996-11, Vol.271 (46), p.29191-29197</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c431t-504fe5d781e42b64ee3325525ef4174c25cc4801bac0724484505c16a2a023153</citedby><cites>FETCH-LOGICAL-c431t-504fe5d781e42b64ee3325525ef4174c25cc4801bac0724484505c16a2a023153</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8910576$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bottger, G</creatorcontrib><creatorcontrib>Nagelkerken, B</creatorcontrib><creatorcontrib>van der Sluijs, P</creatorcontrib><title>Rab4 and Rab7 Define Distinct Nonoverlapping Endosomal Compartments</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Several Rab GTPases have been localized to distinct compartments of the endocytic pathway. Rab4 is associated with early endosomes
and recycling vesicles and regulates membrane recycling from early endosomes. Rab7 is localized to late endosomes and is involved
in the regulation of membrane transport between late endosomes and lysosomes. Although Rab4 and Rab7 appear to regulate distinct
transport events in endocytosis, it is not clear whether they perform their activities in related or entirely distinct intracellular
compartments. To address this question, we generated stable cell lines expressing Rab4 tagged with a novel X31 influenza hemagglutinin
(NH) epitope tag. These antibodies are characterized in this paper and were used to immunoisolate endocytic vesicles with
cytoplasmically exposed NHRab4. Immunoisolated membranes contain internalized 125 I-transferrin, but are devoid of Rab7. Confocal immunofluorescence microscopy showed that the early endosomal GTPases Rab4
and Rab5 both do not codistribute with Rab7 within the same cell. These observations suggest that each of the three Rab GTPases
operationally defines a distinct station of the endocytic pathway.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Cell Compartmentation</subject><subject>CHO Cells</subject><subject>Cricetinae</subject><subject>Dogs</subject><subject>Endocytosis</subject><subject>Endosomes - metabolism</subject><subject>GTP-Binding Proteins - metabolism</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Iodine Radioisotopes</subject><subject>Microscopy, Confocal</subject><subject>Microscopy, Fluorescence</subject><subject>Molecular Sequence Data</subject><subject>rab GTP-Binding Proteins</subject><subject>rab4 GTP-Binding Proteins</subject><subject>Transfection</subject><subject>Transferrin - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkM1LwzAYxoMoc07vXoQexFtr3jTpx1G6-QFDQRS8hTR9u2W0TU06xf_e6obge3leeD4OP0LOgUZAU369KXXEUoh4ErEccjggU6BZHMYC3g7JlFIGYc5EdkxOvN_Q8XgOEzLJcqAiTaakeFYlD1RXBeOTBnOsTYfB3PjBdHoIHm1nP9A1qu9NtwoWXWW9bVUTFLbtlRta7AZ_So5q1Xg82-uMvN4uXor7cPl091DcLEPNYxhCQXmNokozQM7KhCPGMROCCaw5pFwzoTXPKJRK05RxnnFBhYZEMUVZDCKekavdbu_s-xb9IFvjNTaN6tBuvUwzwYDl8Riku6B21nuHteydaZX7kkDlDzc5cpMjN8kT-cttrFzst7dli9VfYQ9q9C93_tqs1p_GoSyN1Wts_898A4ChcuY</recordid><startdate>19961115</startdate><enddate>19961115</enddate><creator>Bottger, G</creator><creator>Nagelkerken, B</creator><creator>van der Sluijs, P</creator><general>American Society for Biochemistry and Molecular Biology</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>7X8</scope></search><sort><creationdate>19961115</creationdate><title>Rab4 and Rab7 Define Distinct Nonoverlapping Endosomal Compartments</title><author>Bottger, G ; Nagelkerken, B ; van der Sluijs, P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c431t-504fe5d781e42b64ee3325525ef4174c25cc4801bac0724484505c16a2a023153</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Cell Compartmentation</topic><topic>CHO Cells</topic><topic>Cricetinae</topic><topic>Dogs</topic><topic>Endocytosis</topic><topic>Endosomes - metabolism</topic><topic>GTP-Binding Proteins - metabolism</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Iodine Radioisotopes</topic><topic>Microscopy, Confocal</topic><topic>Microscopy, Fluorescence</topic><topic>Molecular Sequence Data</topic><topic>rab GTP-Binding Proteins</topic><topic>rab4 GTP-Binding Proteins</topic><topic>Transfection</topic><topic>Transferrin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bottger, G</creatorcontrib><creatorcontrib>Nagelkerken, B</creatorcontrib><creatorcontrib>van der Sluijs, P</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bottger, G</au><au>Nagelkerken, B</au><au>van der Sluijs, P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Rab4 and Rab7 Define Distinct Nonoverlapping Endosomal Compartments</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1996-11-15</date><risdate>1996</risdate><volume>271</volume><issue>46</issue><spage>29191</spage><epage>29197</epage><pages>29191-29197</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Several Rab GTPases have been localized to distinct compartments of the endocytic pathway. Rab4 is associated with early endosomes
and recycling vesicles and regulates membrane recycling from early endosomes. Rab7 is localized to late endosomes and is involved
in the regulation of membrane transport between late endosomes and lysosomes. Although Rab4 and Rab7 appear to regulate distinct
transport events in endocytosis, it is not clear whether they perform their activities in related or entirely distinct intracellular
compartments. To address this question, we generated stable cell lines expressing Rab4 tagged with a novel X31 influenza hemagglutinin
(NH) epitope tag. These antibodies are characterized in this paper and were used to immunoisolate endocytic vesicles with
cytoplasmically exposed NHRab4. Immunoisolated membranes contain internalized 125 I-transferrin, but are devoid of Rab7. Confocal immunofluorescence microscopy showed that the early endosomal GTPases Rab4
and Rab5 both do not codistribute with Rab7 within the same cell. These observations suggest that each of the three Rab GTPases
operationally defines a distinct station of the endocytic pathway.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8910576</pmid><doi>10.1074/jbc.271.46.29191</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1996-11, Vol.271 (46), p.29191-29197 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | MEDLINE; Alma/SFX Local Collection; EZB Electronic Journals Library |
| subjects | Amino Acid Sequence Animals Cell Compartmentation CHO Cells Cricetinae Dogs Endocytosis Endosomes - metabolism GTP-Binding Proteins - metabolism HeLa Cells Humans Iodine Radioisotopes Microscopy, Confocal Microscopy, Fluorescence Molecular Sequence Data rab GTP-Binding Proteins rab4 GTP-Binding Proteins Transfection Transferrin - metabolism |
| title | Rab4 and Rab7 Define Distinct Nonoverlapping Endosomal Compartments |
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