Association of Endophilin B1 with Cytoplasmic Vesicles
Endophilins are SH3- and BAR domain-containing proteins implicated in membrane remodeling and vesicle formation. Endophilins A1 and A2 promote the budding of endocytic vesicles from the plasma membrane, whereas endophilin B1 has been implicated in vesicle budding from intracellular organelles, inclu...
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| Veröffentlicht in: | Biophysical journal 2016-08, Vol.111 (3), p.565-576 |
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| creator | Li, Jinhui Barylko, Barbara Eichorst, John P. Mueller, Joachim D. Albanesi, Joseph P. Chen, Yan |
| description | Endophilins are SH3- and BAR domain-containing proteins implicated in membrane remodeling and vesicle formation. Endophilins A1 and A2 promote the budding of endocytic vesicles from the plasma membrane, whereas endophilin B1 has been implicated in vesicle budding from intracellular organelles, including the trans-Golgi network and late endosomes. We previously reported that endophilins A1 and A2 exist almost exclusively as soluble dimers in the cytosol. Here, we present results of fluorescence fluctuation spectroscopy analyses indicating that, in contrast, the majority of endophilin B1 is present in multiple copies on small, highly mobile cytoplasmic vesicles. Formation of these vesicles was enhanced by overexpression of wild-type dynamin 2, but suppressed by expression of a catalytically inactive dynamin 2 mutant. Using dual-color heterospecies partition analysis, we identified the epidermal growth factor receptor on endophilin B1 vesicles. Moreover, a proportion of endophilin B1 vesicles also contained caveolin, whereas clathrin was almost undetectable on those vesicles. These results raise the possibility that endophilin B1 participates in dynamin 2-dependent formation of a population of transport vesicles distinct from those generated by A-type endophilins. |
| doi_str_mv | 10.1016/j.bpj.2016.06.017 |
| format | Article |
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Endophilins A1 and A2 promote the budding of endocytic vesicles from the plasma membrane, whereas endophilin B1 has been implicated in vesicle budding from intracellular organelles, including the trans-Golgi network and late endosomes. We previously reported that endophilins A1 and A2 exist almost exclusively as soluble dimers in the cytosol. Here, we present results of fluorescence fluctuation spectroscopy analyses indicating that, in contrast, the majority of endophilin B1 is present in multiple copies on small, highly mobile cytoplasmic vesicles. Formation of these vesicles was enhanced by overexpression of wild-type dynamin 2, but suppressed by expression of a catalytically inactive dynamin 2 mutant. Using dual-color heterospecies partition analysis, we identified the epidermal growth factor receptor on endophilin B1 vesicles. Moreover, a proportion of endophilin B1 vesicles also contained caveolin, whereas clathrin was almost undetectable on those vesicles. These results raise the possibility that endophilin B1 participates in dynamin 2-dependent formation of a population of transport vesicles distinct from those generated by A-type endophilins.</description><identifier>ISSN: 0006-3495</identifier><identifier>EISSN: 1542-0086</identifier><identifier>DOI: 10.1016/j.bpj.2016.06.017</identifier><identifier>PMID: 27508440</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adaptor Proteins, Signal Transducing - metabolism ; Animals ; Caveolins - metabolism ; Cell Biophysics ; Cell Line ; Cytoplasm ; Cytoplasmic Vesicles - metabolism ; Dynamin III - metabolism ; Fluorescence ; Humans ; Ligands ; Membranes ; Plasma ; Protein Binding ; Protein Transport ; Proteins ; Rats ; Receptor, Epidermal Growth Factor - metabolism ; Spectrum analysis</subject><ispartof>Biophysical journal, 2016-08, Vol.111 (3), p.565-576</ispartof><rights>2016</rights><rights>Copyright © 2016. Published by Elsevier Inc.</rights><rights>Copyright Biophysical Society Aug 9, 2016</rights><rights>2016. 2016</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c549t-7a1a912ec37ddfcc2d9a77149a38128bddbb9f9620cb81ae6eefdfeba19564143</citedby><cites>FETCH-LOGICAL-c549t-7a1a912ec37ddfcc2d9a77149a38128bddbb9f9620cb81ae6eefdfeba19564143</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4982929/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bpj.2016.06.017$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,724,777,781,882,3537,27905,27906,45976,53772,53774</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27508440$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Li, Jinhui</creatorcontrib><creatorcontrib>Barylko, Barbara</creatorcontrib><creatorcontrib>Eichorst, John P.</creatorcontrib><creatorcontrib>Mueller, Joachim D.</creatorcontrib><creatorcontrib>Albanesi, Joseph P.</creatorcontrib><creatorcontrib>Chen, Yan</creatorcontrib><title>Association of Endophilin B1 with Cytoplasmic Vesicles</title><title>Biophysical journal</title><addtitle>Biophys J</addtitle><description>Endophilins are SH3- and BAR domain-containing proteins implicated in membrane remodeling and vesicle formation. Endophilins A1 and A2 promote the budding of endocytic vesicles from the plasma membrane, whereas endophilin B1 has been implicated in vesicle budding from intracellular organelles, including the trans-Golgi network and late endosomes. We previously reported that endophilins A1 and A2 exist almost exclusively as soluble dimers in the cytosol. Here, we present results of fluorescence fluctuation spectroscopy analyses indicating that, in contrast, the majority of endophilin B1 is present in multiple copies on small, highly mobile cytoplasmic vesicles. Formation of these vesicles was enhanced by overexpression of wild-type dynamin 2, but suppressed by expression of a catalytically inactive dynamin 2 mutant. Using dual-color heterospecies partition analysis, we identified the epidermal growth factor receptor on endophilin B1 vesicles. Moreover, a proportion of endophilin B1 vesicles also contained caveolin, whereas clathrin was almost undetectable on those vesicles. These results raise the possibility that endophilin B1 participates in dynamin 2-dependent formation of a population of transport vesicles distinct from those generated by A-type endophilins.</description><subject>Adaptor Proteins, Signal Transducing - metabolism</subject><subject>Animals</subject><subject>Caveolins - metabolism</subject><subject>Cell Biophysics</subject><subject>Cell Line</subject><subject>Cytoplasm</subject><subject>Cytoplasmic Vesicles - metabolism</subject><subject>Dynamin III - metabolism</subject><subject>Fluorescence</subject><subject>Humans</subject><subject>Ligands</subject><subject>Membranes</subject><subject>Plasma</subject><subject>Protein Binding</subject><subject>Protein Transport</subject><subject>Proteins</subject><subject>Rats</subject><subject>Receptor, Epidermal Growth Factor - metabolism</subject><subject>Spectrum analysis</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kU1rHDEMhk1oaDZpf0AuZaCXXmYreTwfplBIl3wUArm0vRqPrel6mB1P7NmE_Pt42SSkPQQEEujRi6SXsVOEJQJWX_tlO_VLnsolpMD6gC2wFDwHaKp3bAEAVV4IWR6x4xh7AOQl4Ht2xOsSGiFgwaqzGL1xenZ-zHyXnY_WT2s3uDH7gdm9m9fZ6mH206DjxpnsD0VnBoof2GGnh0gfn_IJ-31x_mt1lV_fXP5cnV3nphRyzmuNWiInU9TWdsZwK3Vdo5C6aJA3rbVtKztZcTBtg5oqos521GqUZSVQFCfs-1532rYbsobGOehBTcFtdHhQXjv1b2d0a_XX3ykhGy65TAJfngSCv91SnNXGRUPDoEfy26iwQUxgLTChn_9De78NYzpvRxUVFI0oEoV7ygQfY6DuZRkEtXNF9Sq5onauKEiBdZr59PqKl4lnGxLwbQ9Q-uWdo6CicTQasi6QmZX17g35R8Z7nXY</recordid><startdate>20160809</startdate><enddate>20160809</enddate><creator>Li, Jinhui</creator><creator>Barylko, Barbara</creator><creator>Eichorst, John P.</creator><creator>Mueller, Joachim D.</creator><creator>Albanesi, Joseph P.</creator><creator>Chen, Yan</creator><general>Elsevier Inc</general><general>Biophysical Society</general><general>The Biophysical Society</general><scope>6I.</scope><scope>AAFTH</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>7QO</scope><scope>7QP</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20160809</creationdate><title>Association of Endophilin B1 with Cytoplasmic Vesicles</title><author>Li, Jinhui ; Barylko, Barbara ; Eichorst, John P. ; Mueller, Joachim D. ; Albanesi, Joseph P. ; Chen, Yan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c549t-7a1a912ec37ddfcc2d9a77149a38128bddbb9f9620cb81ae6eefdfeba19564143</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Adaptor Proteins, Signal Transducing - metabolism</topic><topic>Animals</topic><topic>Caveolins - metabolism</topic><topic>Cell Biophysics</topic><topic>Cell Line</topic><topic>Cytoplasm</topic><topic>Cytoplasmic Vesicles - metabolism</topic><topic>Dynamin III - metabolism</topic><topic>Fluorescence</topic><topic>Humans</topic><topic>Ligands</topic><topic>Membranes</topic><topic>Plasma</topic><topic>Protein Binding</topic><topic>Protein Transport</topic><topic>Proteins</topic><topic>Rats</topic><topic>Receptor, Epidermal Growth Factor - metabolism</topic><topic>Spectrum analysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Li, Jinhui</creatorcontrib><creatorcontrib>Barylko, Barbara</creatorcontrib><creatorcontrib>Eichorst, John P.</creatorcontrib><creatorcontrib>Mueller, Joachim D.</creatorcontrib><creatorcontrib>Albanesi, Joseph P.</creatorcontrib><creatorcontrib>Chen, Yan</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biophysical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Li, Jinhui</au><au>Barylko, Barbara</au><au>Eichorst, John P.</au><au>Mueller, Joachim D.</au><au>Albanesi, Joseph P.</au><au>Chen, Yan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Association of Endophilin B1 with Cytoplasmic Vesicles</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>2016-08-09</date><risdate>2016</risdate><volume>111</volume><issue>3</issue><spage>565</spage><epage>576</epage><pages>565-576</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><abstract>Endophilins are SH3- and BAR domain-containing proteins implicated in membrane remodeling and vesicle formation. Endophilins A1 and A2 promote the budding of endocytic vesicles from the plasma membrane, whereas endophilin B1 has been implicated in vesicle budding from intracellular organelles, including the trans-Golgi network and late endosomes. We previously reported that endophilins A1 and A2 exist almost exclusively as soluble dimers in the cytosol. Here, we present results of fluorescence fluctuation spectroscopy analyses indicating that, in contrast, the majority of endophilin B1 is present in multiple copies on small, highly mobile cytoplasmic vesicles. Formation of these vesicles was enhanced by overexpression of wild-type dynamin 2, but suppressed by expression of a catalytically inactive dynamin 2 mutant. Using dual-color heterospecies partition analysis, we identified the epidermal growth factor receptor on endophilin B1 vesicles. Moreover, a proportion of endophilin B1 vesicles also contained caveolin, whereas clathrin was almost undetectable on those vesicles. 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| source | MEDLINE; Cell Press Free Archives; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | Adaptor Proteins, Signal Transducing - metabolism Animals Caveolins - metabolism Cell Biophysics Cell Line Cytoplasm Cytoplasmic Vesicles - metabolism Dynamin III - metabolism Fluorescence Humans Ligands Membranes Plasma Protein Binding Protein Transport Proteins Rats Receptor, Epidermal Growth Factor - metabolism Spectrum analysis |
| title | Association of Endophilin B1 with Cytoplasmic Vesicles |
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