Hrs-2 Regulates Receptor-mediated Endocytosis via Interactions with Eps15
Hrs-2, via interactions with SNAP-25, plays a regulatory role on the exocytic machinery. We now show that Hrs-2 physically interacts with Eps15, a protein required for receptor-mediated endocytosis. The Hrs-2/Eps15 interaction is calcium dependent, inhibited by SNAP-25 and α-adaptin, and results in...
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| Veröffentlicht in: | The Journal of biological chemistry 2000-05, Vol.275 (20), p.15271-15278 |
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| container_end_page | 15278 |
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| container_issue | 20 |
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| container_title | The Journal of biological chemistry |
| container_volume | 275 |
| creator | Bean, Andrew J. Davanger, Svend Chou, Marian F. Gerhardt, Brenda Tsujimoto, Susan Chang, YuChieh |
| description | Hrs-2, via interactions with SNAP-25, plays a regulatory role on the exocytic machinery. We now show that Hrs-2 physically interacts with Eps15, a protein required for receptor-mediated endocytosis. The Hrs-2/Eps15 interaction is calcium dependent, inhibited by SNAP-25 and α-adaptin, and results in the inhibition of receptor-mediated endocytosis. Immunoelectron microscopy reveals Hrs-2 localization on the limiting membrane of multivesicular bodies, organelles in the endosomal pathway. These data show that Hrs-2 regulates endocytosis, delineate a biochemical pathway (Hrs-2-Eps15-AP2) in which Hrs-2 functions, and suggest that Hrs-2 acts to provide communication between endo- and exocytic processes. |
| doi_str_mv | 10.1074/jbc.275.20.15271 |
| format | Article |
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We now show that Hrs-2 physically interacts with Eps15, a protein required for receptor-mediated endocytosis. The Hrs-2/Eps15 interaction is calcium dependent, inhibited by SNAP-25 and α-adaptin, and results in the inhibition of receptor-mediated endocytosis. Immunoelectron microscopy reveals Hrs-2 localization on the limiting membrane of multivesicular bodies, organelles in the endosomal pathway. These data show that Hrs-2 regulates endocytosis, delineate a biochemical pathway (Hrs-2-Eps15-AP2) in which Hrs-2 functions, and suggest that Hrs-2 acts to provide communication between endo- and exocytic processes.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.275.20.15271</identifier><identifier>PMID: 10809762</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adaptor Proteins, Signal Transducing ; Adenosine Triphosphatases - analysis ; Adenosine Triphosphatases - metabolism ; Animals ; Brain - metabolism ; Calcium - metabolism ; Calcium-Binding Proteins - metabolism ; Cerebellum - metabolism ; Endocytosis - physiology ; Endosomal Sorting Complexes Required for Transport ; Endosomes - metabolism ; Endosomes - ultrastructure ; HeLa Cells ; Humans ; Intracellular Signaling Peptides and Proteins ; Kinetics ; Membrane Proteins ; Microscopy, Immunoelectron ; Nerve Tissue Proteins - metabolism ; Neurons - metabolism ; Neurons - ultrastructure ; Phosphoproteins - metabolism ; Rats ; Receptors, Cell Surface - physiology ; Recombinant Proteins - metabolism ; Signal Transduction ; Synaptosomal-Associated Protein 25</subject><ispartof>The Journal of biological chemistry, 2000-05, Vol.275 (20), p.15271-15278</ispartof><rights>2000 © 2000 ASBMB. 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We now show that Hrs-2 physically interacts with Eps15, a protein required for receptor-mediated endocytosis. The Hrs-2/Eps15 interaction is calcium dependent, inhibited by SNAP-25 and α-adaptin, and results in the inhibition of receptor-mediated endocytosis. Immunoelectron microscopy reveals Hrs-2 localization on the limiting membrane of multivesicular bodies, organelles in the endosomal pathway. These data show that Hrs-2 regulates endocytosis, delineate a biochemical pathway (Hrs-2-Eps15-AP2) in which Hrs-2 functions, and suggest that Hrs-2 acts to provide communication between endo- and exocytic processes.</description><subject>Adaptor Proteins, Signal Transducing</subject><subject>Adenosine Triphosphatases - analysis</subject><subject>Adenosine Triphosphatases - metabolism</subject><subject>Animals</subject><subject>Brain - metabolism</subject><subject>Calcium - metabolism</subject><subject>Calcium-Binding Proteins - metabolism</subject><subject>Cerebellum - metabolism</subject><subject>Endocytosis - physiology</subject><subject>Endosomal Sorting Complexes Required for Transport</subject><subject>Endosomes - metabolism</subject><subject>Endosomes - ultrastructure</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Intracellular Signaling Peptides and Proteins</subject><subject>Kinetics</subject><subject>Membrane Proteins</subject><subject>Microscopy, Immunoelectron</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Neurons - metabolism</subject><subject>Neurons - ultrastructure</subject><subject>Phosphoproteins - metabolism</subject><subject>Rats</subject><subject>Receptors, Cell Surface - physiology</subject><subject>Recombinant Proteins - metabolism</subject><subject>Signal Transduction</subject><subject>Synaptosomal-Associated Protein 25</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kMFLwzAUh4MoOqd3T9KDeOvMS5tm9SYydTAQRMFbSJM3F1mbmaQO_3sj3UEEc3l5j-_9SD5CzoBOgIry6r3REyb4hKWeMwF7ZAR0WuQFh9d9MqKUQV4zPj0ixyG803TKGg7JUYJoLSo2IvMHH3KWPeFbv1YRQ7pp3ETn8xaNTROTzTrj9Fd0wYbs06ps3kX0SkfrupBtbVxls00AfkIOlmod8HRXx-TlbvZ8-5AvHu_ntzeLXJcgYq7qmlPRMDTLmhsQQlWlNjAtkJVG82paMoQKjQKGTaWUKBpRojDIgAtW0WJMLofcjXcfPYYoWxs0rteqQ9cHKQCgThISSAdQexeCx6XceNsq_yWByh99MumTSZ9kqf_Rl1bOd9l9k_7_a2HwlYCLAVjZt9XWepSNdXqF7d-c6wHDJOLTopdBW-x0UupRR2mc_f8R3zVwie0</recordid><startdate>20000519</startdate><enddate>20000519</enddate><creator>Bean, Andrew J.</creator><creator>Davanger, Svend</creator><creator>Chou, Marian F.</creator><creator>Gerhardt, Brenda</creator><creator>Tsujimoto, Susan</creator><creator>Chang, YuChieh</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</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>7X8</scope></search><sort><creationdate>20000519</creationdate><title>Hrs-2 Regulates Receptor-mediated Endocytosis via Interactions with Eps15</title><author>Bean, Andrew J. ; Davanger, Svend ; Chou, Marian F. ; Gerhardt, Brenda ; Tsujimoto, Susan ; Chang, YuChieh</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c417t-a99507b2edf95d177a64cd183e24dc56842e16eda12eb6aa73b74e7de21572603</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Adaptor Proteins, Signal Transducing</topic><topic>Adenosine Triphosphatases - analysis</topic><topic>Adenosine Triphosphatases - metabolism</topic><topic>Animals</topic><topic>Brain - metabolism</topic><topic>Calcium - metabolism</topic><topic>Calcium-Binding Proteins - metabolism</topic><topic>Cerebellum - metabolism</topic><topic>Endocytosis - physiology</topic><topic>Endosomal Sorting Complexes Required for Transport</topic><topic>Endosomes - metabolism</topic><topic>Endosomes - ultrastructure</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Intracellular Signaling Peptides and Proteins</topic><topic>Kinetics</topic><topic>Membrane Proteins</topic><topic>Microscopy, Immunoelectron</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Neurons - metabolism</topic><topic>Neurons - ultrastructure</topic><topic>Phosphoproteins - metabolism</topic><topic>Rats</topic><topic>Receptors, Cell Surface - physiology</topic><topic>Recombinant Proteins - metabolism</topic><topic>Signal Transduction</topic><topic>Synaptosomal-Associated Protein 25</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bean, Andrew J.</creatorcontrib><creatorcontrib>Davanger, Svend</creatorcontrib><creatorcontrib>Chou, Marian F.</creatorcontrib><creatorcontrib>Gerhardt, Brenda</creatorcontrib><creatorcontrib>Tsujimoto, Susan</creatorcontrib><creatorcontrib>Chang, YuChieh</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>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bean, Andrew J.</au><au>Davanger, Svend</au><au>Chou, Marian F.</au><au>Gerhardt, Brenda</au><au>Tsujimoto, Susan</au><au>Chang, YuChieh</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Hrs-2 Regulates Receptor-mediated Endocytosis via Interactions with Eps15</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2000-05-19</date><risdate>2000</risdate><volume>275</volume><issue>20</issue><spage>15271</spage><epage>15278</epage><pages>15271-15278</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Hrs-2, via interactions with SNAP-25, plays a regulatory role on the exocytic machinery. We now show that Hrs-2 physically interacts with Eps15, a protein required for receptor-mediated endocytosis. The Hrs-2/Eps15 interaction is calcium dependent, inhibited by SNAP-25 and α-adaptin, and results in the inhibition of receptor-mediated endocytosis. Immunoelectron microscopy reveals Hrs-2 localization on the limiting membrane of multivesicular bodies, organelles in the endosomal pathway. These data show that Hrs-2 regulates endocytosis, delineate a biochemical pathway (Hrs-2-Eps15-AP2) in which Hrs-2 functions, and suggest that Hrs-2 acts to provide communication between endo- and exocytic processes.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>10809762</pmid><doi>10.1074/jbc.275.20.15271</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adaptor Proteins, Signal Transducing Adenosine Triphosphatases - analysis Adenosine Triphosphatases - metabolism Animals Brain - metabolism Calcium - metabolism Calcium-Binding Proteins - metabolism Cerebellum - metabolism Endocytosis - physiology Endosomal Sorting Complexes Required for Transport Endosomes - metabolism Endosomes - ultrastructure HeLa Cells Humans Intracellular Signaling Peptides and Proteins Kinetics Membrane Proteins Microscopy, Immunoelectron Nerve Tissue Proteins - metabolism Neurons - metabolism Neurons - ultrastructure Phosphoproteins - metabolism Rats Receptors, Cell Surface - physiology Recombinant Proteins - metabolism Signal Transduction Synaptosomal-Associated Protein 25 |
| title | Hrs-2 Regulates Receptor-mediated Endocytosis via Interactions with Eps15 |
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