Rab5a and rab11a mediate agonist-induced trafficking of protease-activated receptor 2
Departments of Surgery and Physiology, University of California, San Francisco, California 94143-0660 We evaluated the contribution of rab5a and rab11a to trafficking and signaling of protease-activated receptor 2 (PAR2), a receptor for trypsin and tryptase. Agonists stimulated internalization of PA...
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| Veröffentlicht in: | American Journal of Physiology: Cell Physiology 2003-05, Vol.284 (5), p.C1319-C1329 |
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| container_title | American Journal of Physiology: Cell Physiology |
| container_volume | 284 |
| creator | Roosterman, Dirk Schmidlin, Fabien Bunnett, Nigel W |
| description | Departments of Surgery and Physiology, University of
California, San Francisco, California 94143-0660
We evaluated the contribution of
rab5a and rab11a to trafficking and signaling of protease-activated
receptor 2 (PAR2), a receptor for trypsin and tryptase. Agonists
stimulated internalization of PAR2 into early endosomes containing
rab5a. Dominant negative rab5aS34N disrupted early endosomes and
inhibited agonist-stimulated endocytosis of PAR2. Internalized PAR2 was
sorted to lysosomes, and rab5a remained in early endosomes. Rab5a
promoted and rab5aS34N impeded resensitization of trypsin-induced
calcium mobilization. Rab11a was detected in the Golgi apparatus with
PAR2, and PAR2 agonists stimulated redistribution of rab11a into
vesicles containing PAR2 that migrated to the cell surface. Dominant
negative rab11aS25N was mostly confined to the Golgi apparatus.
Although expression of rab11aS25N caused retention of PAR2 in the Golgi
apparatus, it did not abolish trafficking of PAR2 to the cell surface.
However, expression of wild-type rab11a accelerated both recovery of
PAR2 at the cell surface and resensitization of PAR2 signaling. Thus rab5a is required for PAR2 endocytosis and resensitization, whereas rab11a contributes to trafficking of PAR2 from the Golgi apparatus to
the plasma membrane.
desensitization; resensitization; internalization; recycling; GTPases |
| doi_str_mv | 10.1152/ajpcell.00540.2002 |
| format | Article |
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California, San Francisco, California 94143-0660
We evaluated the contribution of
rab5a and rab11a to trafficking and signaling of protease-activated
receptor 2 (PAR2), a receptor for trypsin and tryptase. Agonists
stimulated internalization of PAR2 into early endosomes containing
rab5a. Dominant negative rab5aS34N disrupted early endosomes and
inhibited agonist-stimulated endocytosis of PAR2. Internalized PAR2 was
sorted to lysosomes, and rab5a remained in early endosomes. Rab5a
promoted and rab5aS34N impeded resensitization of trypsin-induced
calcium mobilization. Rab11a was detected in the Golgi apparatus with
PAR2, and PAR2 agonists stimulated redistribution of rab11a into
vesicles containing PAR2 that migrated to the cell surface. Dominant
negative rab11aS25N was mostly confined to the Golgi apparatus.
Although expression of rab11aS25N caused retention of PAR2 in the Golgi
apparatus, it did not abolish trafficking of PAR2 to the cell surface.
However, expression of wild-type rab11a accelerated both recovery of
PAR2 at the cell surface and resensitization of PAR2 signaling. Thus rab5a is required for PAR2 endocytosis and resensitization, whereas rab11a contributes to trafficking of PAR2 from the Golgi apparatus to
the plasma membrane.
desensitization; resensitization; internalization; recycling; GTPases</description><identifier>ISSN: 0363-6143</identifier><identifier>EISSN: 1522-1563</identifier><identifier>DOI: 10.1152/ajpcell.00540.2002</identifier><identifier>PMID: 12540381</identifier><language>eng</language><publisher>United States</publisher><subject>Animals ; Cell Line ; Endocytosis - physiology ; Humans ; Protein Transport - physiology ; rab GTP-Binding Proteins - physiology ; rab5 GTP-Binding Proteins - physiology ; Rats ; Receptor, PAR-2 ; Receptors, Thrombin - agonists ; Receptors, Thrombin - metabolism ; Signal Transduction - physiology ; Tissue Distribution</subject><ispartof>American Journal of Physiology: Cell Physiology, 2003-05, Vol.284 (5), p.C1319-C1329</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c455t-e78b6d7982536024ae6316d46fd5625a3abf2fc71b149cdda4b547066b874fcc3</citedby><cites>FETCH-LOGICAL-c455t-e78b6d7982536024ae6316d46fd5625a3abf2fc71b149cdda4b547066b874fcc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,3026,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12540381$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Roosterman, Dirk</creatorcontrib><creatorcontrib>Schmidlin, Fabien</creatorcontrib><creatorcontrib>Bunnett, Nigel W</creatorcontrib><title>Rab5a and rab11a mediate agonist-induced trafficking of protease-activated receptor 2</title><title>American Journal of Physiology: Cell Physiology</title><addtitle>Am J Physiol Cell Physiol</addtitle><description>Departments of Surgery and Physiology, University of
California, San Francisco, California 94143-0660
We evaluated the contribution of
rab5a and rab11a to trafficking and signaling of protease-activated
receptor 2 (PAR2), a receptor for trypsin and tryptase. Agonists
stimulated internalization of PAR2 into early endosomes containing
rab5a. Dominant negative rab5aS34N disrupted early endosomes and
inhibited agonist-stimulated endocytosis of PAR2. Internalized PAR2 was
sorted to lysosomes, and rab5a remained in early endosomes. Rab5a
promoted and rab5aS34N impeded resensitization of trypsin-induced
calcium mobilization. Rab11a was detected in the Golgi apparatus with
PAR2, and PAR2 agonists stimulated redistribution of rab11a into
vesicles containing PAR2 that migrated to the cell surface. Dominant
negative rab11aS25N was mostly confined to the Golgi apparatus.
Although expression of rab11aS25N caused retention of PAR2 in the Golgi
apparatus, it did not abolish trafficking of PAR2 to the cell surface.
However, expression of wild-type rab11a accelerated both recovery of
PAR2 at the cell surface and resensitization of PAR2 signaling. Thus rab5a is required for PAR2 endocytosis and resensitization, whereas rab11a contributes to trafficking of PAR2 from the Golgi apparatus to
the plasma membrane.
desensitization; resensitization; internalization; recycling; GTPases</description><subject>Animals</subject><subject>Cell Line</subject><subject>Endocytosis - physiology</subject><subject>Humans</subject><subject>Protein Transport - physiology</subject><subject>rab GTP-Binding Proteins - physiology</subject><subject>rab5 GTP-Binding Proteins - physiology</subject><subject>Rats</subject><subject>Receptor, PAR-2</subject><subject>Receptors, Thrombin - agonists</subject><subject>Receptors, Thrombin - metabolism</subject><subject>Signal Transduction - physiology</subject><subject>Tissue Distribution</subject><issn>0363-6143</issn><issn>1522-1563</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kEtvEzEURi1ERUPLH2CBZsVugq9fM2GHIkqRKiFV7dq640fiMpkZbE8h_x6nCY9NV17c7xxZh5C3QJcAkn3Ah8m4vl9SKgVdMkrZC7IoB1aDVPwlWVCueK1A8HPyOqUHSqlgavWKnAMrBG9hQe5vsZNY4WCriB0AVjtnA2ZX4WYcQsp1GOxsnK1yRO-D-R6GTTX6aopjdphcjSaHxwIUgTNuymOs2CU589gn9-b0XpD7q8936-v65tuXr-tPN7URUubaNW2nbLNqmeSKMoFOcVBWKG-lYhI5dp5500AHYmWsRdFJ0VClurYR3hh-Qd4fveU3P2aXst6FdGiCgxvnpBsODXBOy5AdhyaOKUXn9RTDDuNeA9WHmPoUUz_F1IeYBXp3ss9dqfIPOdUrg-VxsA2b7c8QnZ62-xTGftzs_wpZK7TUa-CwKsDH54Grue_v3K_8h_wP1JP1_Dc5SZa6</recordid><startdate>20030501</startdate><enddate>20030501</enddate><creator>Roosterman, Dirk</creator><creator>Schmidlin, Fabien</creator><creator>Bunnett, Nigel W</creator><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>20030501</creationdate><title>Rab5a and rab11a mediate agonist-induced trafficking of protease-activated receptor 2</title><author>Roosterman, Dirk ; Schmidlin, Fabien ; Bunnett, Nigel W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c455t-e78b6d7982536024ae6316d46fd5625a3abf2fc71b149cdda4b547066b874fcc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Animals</topic><topic>Cell Line</topic><topic>Endocytosis - physiology</topic><topic>Humans</topic><topic>Protein Transport - physiology</topic><topic>rab GTP-Binding Proteins - physiology</topic><topic>rab5 GTP-Binding Proteins - physiology</topic><topic>Rats</topic><topic>Receptor, PAR-2</topic><topic>Receptors, Thrombin - agonists</topic><topic>Receptors, Thrombin - metabolism</topic><topic>Signal Transduction - physiology</topic><topic>Tissue Distribution</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Roosterman, Dirk</creatorcontrib><creatorcontrib>Schmidlin, Fabien</creatorcontrib><creatorcontrib>Bunnett, Nigel W</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>American Journal of Physiology: Cell Physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Roosterman, Dirk</au><au>Schmidlin, Fabien</au><au>Bunnett, Nigel W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Rab5a and rab11a mediate agonist-induced trafficking of protease-activated receptor 2</atitle><jtitle>American Journal of Physiology: Cell Physiology</jtitle><addtitle>Am J Physiol Cell Physiol</addtitle><date>2003-05-01</date><risdate>2003</risdate><volume>284</volume><issue>5</issue><spage>C1319</spage><epage>C1329</epage><pages>C1319-C1329</pages><issn>0363-6143</issn><eissn>1522-1563</eissn><abstract>Departments of Surgery and Physiology, University of
California, San Francisco, California 94143-0660
We evaluated the contribution of
rab5a and rab11a to trafficking and signaling of protease-activated
receptor 2 (PAR2), a receptor for trypsin and tryptase. Agonists
stimulated internalization of PAR2 into early endosomes containing
rab5a. Dominant negative rab5aS34N disrupted early endosomes and
inhibited agonist-stimulated endocytosis of PAR2. Internalized PAR2 was
sorted to lysosomes, and rab5a remained in early endosomes. Rab5a
promoted and rab5aS34N impeded resensitization of trypsin-induced
calcium mobilization. Rab11a was detected in the Golgi apparatus with
PAR2, and PAR2 agonists stimulated redistribution of rab11a into
vesicles containing PAR2 that migrated to the cell surface. Dominant
negative rab11aS25N was mostly confined to the Golgi apparatus.
Although expression of rab11aS25N caused retention of PAR2 in the Golgi
apparatus, it did not abolish trafficking of PAR2 to the cell surface.
However, expression of wild-type rab11a accelerated both recovery of
PAR2 at the cell surface and resensitization of PAR2 signaling. Thus rab5a is required for PAR2 endocytosis and resensitization, whereas rab11a contributes to trafficking of PAR2 from the Golgi apparatus to
the plasma membrane.
desensitization; resensitization; internalization; recycling; GTPases</abstract><cop>United States</cop><pmid>12540381</pmid><doi>10.1152/ajpcell.00540.2002</doi></addata></record> |
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| ispartof | American Journal of Physiology: Cell Physiology, 2003-05, Vol.284 (5), p.C1319-C1329 |
| issn | 0363-6143 1522-1563 |
| language | eng |
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| source | MEDLINE; American Physiological Society; EZB-FREE-00999 freely available EZB journals |
| subjects | Animals Cell Line Endocytosis - physiology Humans Protein Transport - physiology rab GTP-Binding Proteins - physiology rab5 GTP-Binding Proteins - physiology Rats Receptor, PAR-2 Receptors, Thrombin - agonists Receptors, Thrombin - metabolism Signal Transduction - physiology Tissue Distribution |
| title | Rab5a and rab11a mediate agonist-induced trafficking of protease-activated receptor 2 |
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