Stonin 2: An Adaptor-like Protein That Interacts with Components of the Endocytic Machinery
Endocytosis of cell surface proteins is mediated by a complex molecular machinery that assembles on the inner surface of the plasma membrane. Here, we report the identification of two ubiquitously expressed human proteins, stonin 1 and stonin 2, related to components of the endocytic machinery. The...
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| Veröffentlicht in: | The Journal of cell biology 2001-05, Vol.153 (5), p.1111-1120 |
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| creator | Martina, José A. Bonangelino, Cecilia J. Aguilar, Rubén C. Bonifacino, Juan S. |
| description | Endocytosis of cell surface proteins is mediated by a complex molecular machinery that assembles on the inner surface of the plasma membrane. Here, we report the identification of two ubiquitously expressed human proteins, stonin 1 and stonin 2, related to components of the endocytic machinery. The human stonins are homologous to the Drosophila melanogaster stoned B protein and exhibit a modular structure consisting of an NH2-terminal proline-rich domain, a central region of homology specific to the stonins, and a COOH-terminal region homologous to the μ subunits of adaptor protein (AP) complexes. Stonin 2, but not stonin 1, interacts with the endocytic machinery proteins Eps15, Eps15R, and intersectin 1. These interactions occur via two NPF motifs in the proline-rich domain of stonin 2 and Eps15 homology domains of Eps15, Eps15R, and intersectin 1. Stonin 2 also interacts indirectly with the adaptor protein complex, AP-2. In addition, stonin 2 binds to the C2B domains of synaptotagmins I and II. Overexpression of GFP-stonin 2 interferes with recruitment of AP-2 to the plasma membrane and impairs internalization of the transferrin, epidermal growth factor, and low density lipoprotein receptors. These observations suggest that stonin 2 is a novel component of the general endocytic machinery. |
| doi_str_mv | 10.1083/jcb.153.5.1111 |
| format | Article |
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Here, we report the identification of two ubiquitously expressed human proteins, stonin 1 and stonin 2, related to components of the endocytic machinery. The human stonins are homologous to the Drosophila melanogaster stoned B protein and exhibit a modular structure consisting of an NH2-terminal proline-rich domain, a central region of homology specific to the stonins, and a COOH-terminal region homologous to the μ subunits of adaptor protein (AP) complexes. Stonin 2, but not stonin 1, interacts with the endocytic machinery proteins Eps15, Eps15R, and intersectin 1. These interactions occur via two NPF motifs in the proline-rich domain of stonin 2 and Eps15 homology domains of Eps15, Eps15R, and intersectin 1. Stonin 2 also interacts indirectly with the adaptor protein complex, AP-2. In addition, stonin 2 binds to the C2B domains of synaptotagmins I and II. Overexpression of GFP-stonin 2 interferes with recruitment of AP-2 to the plasma membrane and impairs internalization of the transferrin, epidermal growth factor, and low density lipoprotein receptors. These observations suggest that stonin 2 is a novel component of the general endocytic machinery.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.153.5.1111</identifier><identifier>PMID: 11381094</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>Adaptor Protein Complex alpha Subunits ; Adaptor Proteins, Signal Transducing ; Adaptor Proteins, Vesicular Transport ; Amino Acid Sequence ; Amino acids ; Antibodies ; Calcium-Binding Proteins - chemistry ; Calcium-Binding Proteins - genetics ; Calcium-Binding Proteins - metabolism ; Carrier Proteins - chemistry ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Cell biology ; Cell lines ; Cell Membrane - chemistry ; Cell Membrane - metabolism ; Cell membranes ; Cells ; Cytosol - metabolism ; Drosophila Proteins ; Endocytosis ; Endosomes - chemistry ; Endosomes - metabolism ; Epidermal Growth Factor - metabolism ; Gene Expression Profiling ; HeLa cells ; Humans ; Intracellular Signaling Peptides and Proteins ; Membrane Glycoproteins - chemistry ; Membrane Glycoproteins - metabolism ; Membrane Proteins - chemistry ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Membranes ; Molecular Sequence Data ; Molecules ; Nerve Tissue Proteins - chemistry ; Nerve Tissue Proteins - metabolism ; Neurons ; Original ; Phosphoproteins - chemistry ; Phosphoproteins - genetics ; Phosphoproteins - metabolism ; Plasma ; Proline - metabolism ; Protein Binding ; Protein Structure, Tertiary ; Protein Subunits ; Proteins ; Receptors, LDL - metabolism ; Sequence Homology, Amino Acid ; Synaptotagmin II ; Synaptotagmins ; Transcription Factors, General ; Transferrin - metabolism ; Two-Hybrid System Techniques ; Vesicular Transport Proteins</subject><ispartof>The Journal of cell biology, 2001-05, Vol.153 (5), p.1111-1120</ispartof><rights>Copyright 2001 The Rockefeller University Press</rights><rights>Copyright Rockefeller University Press May 28, 2001</rights><rights>2001 The Rockefeller University Press 2001 The Rockefeller University Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11381094$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Martina, José A.</creatorcontrib><creatorcontrib>Bonangelino, Cecilia J.</creatorcontrib><creatorcontrib>Aguilar, Rubén C.</creatorcontrib><creatorcontrib>Bonifacino, Juan S.</creatorcontrib><title>Stonin 2: An Adaptor-like Protein That Interacts with Components of the Endocytic Machinery</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>Endocytosis of cell surface proteins is mediated by a complex molecular machinery that assembles on the inner surface of the plasma membrane. Here, we report the identification of two ubiquitously expressed human proteins, stonin 1 and stonin 2, related to components of the endocytic machinery. The human stonins are homologous to the Drosophila melanogaster stoned B protein and exhibit a modular structure consisting of an NH2-terminal proline-rich domain, a central region of homology specific to the stonins, and a COOH-terminal region homologous to the μ subunits of adaptor protein (AP) complexes. Stonin 2, but not stonin 1, interacts with the endocytic machinery proteins Eps15, Eps15R, and intersectin 1. These interactions occur via two NPF motifs in the proline-rich domain of stonin 2 and Eps15 homology domains of Eps15, Eps15R, and intersectin 1. Stonin 2 also interacts indirectly with the adaptor protein complex, AP-2. In addition, stonin 2 binds to the C2B domains of synaptotagmins I and II. Overexpression of GFP-stonin 2 interferes with recruitment of AP-2 to the plasma membrane and impairs internalization of the transferrin, epidermal growth factor, and low density lipoprotein receptors. These observations suggest that stonin 2 is a novel component of the general endocytic machinery.</description><subject>Adaptor Protein Complex alpha Subunits</subject><subject>Adaptor Proteins, Signal Transducing</subject><subject>Adaptor Proteins, Vesicular Transport</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Antibodies</subject><subject>Calcium-Binding Proteins - chemistry</subject><subject>Calcium-Binding Proteins - genetics</subject><subject>Calcium-Binding Proteins - metabolism</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell biology</subject><subject>Cell lines</subject><subject>Cell Membrane - chemistry</subject><subject>Cell Membrane - metabolism</subject><subject>Cell membranes</subject><subject>Cells</subject><subject>Cytosol - metabolism</subject><subject>Drosophila Proteins</subject><subject>Endocytosis</subject><subject>Endosomes - chemistry</subject><subject>Endosomes - metabolism</subject><subject>Epidermal Growth Factor - metabolism</subject><subject>Gene Expression Profiling</subject><subject>HeLa cells</subject><subject>Humans</subject><subject>Intracellular Signaling Peptides and Proteins</subject><subject>Membrane Glycoproteins - chemistry</subject><subject>Membrane Glycoproteins - metabolism</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Membranes</subject><subject>Molecular Sequence Data</subject><subject>Molecules</subject><subject>Nerve Tissue Proteins - chemistry</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Neurons</subject><subject>Original</subject><subject>Phosphoproteins - chemistry</subject><subject>Phosphoproteins - genetics</subject><subject>Phosphoproteins - metabolism</subject><subject>Plasma</subject><subject>Proline - metabolism</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Protein Subunits</subject><subject>Proteins</subject><subject>Receptors, LDL - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Synaptotagmin II</subject><subject>Synaptotagmins</subject><subject>Transcription Factors, General</subject><subject>Transferrin - metabolism</subject><subject>Two-Hybrid System Techniques</subject><subject>Vesicular Transport Proteins</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkEFvEzEQhS0EomnplROqLA7cNp1Z78ROD0hR1EKlVq1Ebj2sHK-X9XZjB68Dyr-vUQu0zGU0ep-e3jzG3iNMEZQ47c16iiSmNMU8r9gEqYJCYQWv2QSgxGJOJR2ww3HsAaCSlXjLDhCFQphXE3b3LQXvPC_P-MLzRaO3KcRicPeW38aQbJZWnU780icbtUkj_-VSx5dhsw3e-nyHlqfO8nPfBLNPzvBrbTrnbdy_Y29aPYz2-GkfsdXF-Wr5tbi6-XK5XFwVvUBIRdtS0xpLYOZVCetGC4KGiLSSMwRohCKprGgEIaCRZWUQrTY0m-U3lRRH7POj7Xa33tjG5FRRD_U2uo2O-zpoV79UvOvq7-FnXWJuo6Rs8OnJIIYfOzumeuNGY4dBext2Yy1BKSFpnsGP_4F92EWff_vtBVIKUhk6eR7nb44_nWfgwyPQj7nrf_qsBBIgHgA_ToxU</recordid><startdate>20010528</startdate><enddate>20010528</enddate><creator>Martina, José A.</creator><creator>Bonangelino, Cecilia J.</creator><creator>Aguilar, Rubén C.</creator><creator>Bonifacino, Juan S.</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20010528</creationdate><title>Stonin 2: An Adaptor-like Protein That Interacts with Components of the Endocytic Machinery</title><author>Martina, José A. ; Bonangelino, Cecilia J. ; Aguilar, Rubén C. ; Bonifacino, Juan S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-j310t-ff5dfce50c9420bda350d555a876100d38578e3d35101c724c11eac566814873</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Adaptor Protein Complex alpha Subunits</topic><topic>Adaptor Proteins, Signal Transducing</topic><topic>Adaptor Proteins, Vesicular Transport</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Antibodies</topic><topic>Calcium-Binding Proteins - chemistry</topic><topic>Calcium-Binding Proteins - genetics</topic><topic>Calcium-Binding Proteins - metabolism</topic><topic>Carrier Proteins - chemistry</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell biology</topic><topic>Cell lines</topic><topic>Cell Membrane - chemistry</topic><topic>Cell Membrane - metabolism</topic><topic>Cell membranes</topic><topic>Cells</topic><topic>Cytosol - metabolism</topic><topic>Drosophila Proteins</topic><topic>Endocytosis</topic><topic>Endosomes - chemistry</topic><topic>Endosomes - metabolism</topic><topic>Epidermal Growth Factor - metabolism</topic><topic>Gene Expression Profiling</topic><topic>HeLa cells</topic><topic>Humans</topic><topic>Intracellular Signaling Peptides and Proteins</topic><topic>Membrane Glycoproteins - chemistry</topic><topic>Membrane Glycoproteins - metabolism</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Membranes</topic><topic>Molecular Sequence Data</topic><topic>Molecules</topic><topic>Nerve Tissue Proteins - chemistry</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Neurons</topic><topic>Original</topic><topic>Phosphoproteins - chemistry</topic><topic>Phosphoproteins - genetics</topic><topic>Phosphoproteins - metabolism</topic><topic>Plasma</topic><topic>Proline - metabolism</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>Protein Subunits</topic><topic>Proteins</topic><topic>Receptors, LDL - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Synaptotagmin II</topic><topic>Synaptotagmins</topic><topic>Transcription Factors, General</topic><topic>Transferrin - metabolism</topic><topic>Two-Hybrid System Techniques</topic><topic>Vesicular Transport Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Martina, José A.</creatorcontrib><creatorcontrib>Bonangelino, Cecilia J.</creatorcontrib><creatorcontrib>Aguilar, Rubén C.</creatorcontrib><creatorcontrib>Bonifacino, Juan S.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Martina, José A.</au><au>Bonangelino, Cecilia J.</au><au>Aguilar, Rubén C.</au><au>Bonifacino, Juan S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Stonin 2: An Adaptor-like Protein That Interacts with Components of the Endocytic Machinery</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>2001-05-28</date><risdate>2001</risdate><volume>153</volume><issue>5</issue><spage>1111</spage><epage>1120</epage><pages>1111-1120</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>Endocytosis of cell surface proteins is mediated by a complex molecular machinery that assembles on the inner surface of the plasma membrane. Here, we report the identification of two ubiquitously expressed human proteins, stonin 1 and stonin 2, related to components of the endocytic machinery. The human stonins are homologous to the Drosophila melanogaster stoned B protein and exhibit a modular structure consisting of an NH2-terminal proline-rich domain, a central region of homology specific to the stonins, and a COOH-terminal region homologous to the μ subunits of adaptor protein (AP) complexes. Stonin 2, but not stonin 1, interacts with the endocytic machinery proteins Eps15, Eps15R, and intersectin 1. These interactions occur via two NPF motifs in the proline-rich domain of stonin 2 and Eps15 homology domains of Eps15, Eps15R, and intersectin 1. Stonin 2 also interacts indirectly with the adaptor protein complex, AP-2. In addition, stonin 2 binds to the C2B domains of synaptotagmins I and II. Overexpression of GFP-stonin 2 interferes with recruitment of AP-2 to the plasma membrane and impairs internalization of the transferrin, epidermal growth factor, and low density lipoprotein receptors. These observations suggest that stonin 2 is a novel component of the general endocytic machinery.</abstract><cop>United States</cop><pub>Rockefeller University Press</pub><pmid>11381094</pmid><doi>10.1083/jcb.153.5.1111</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adaptor Protein Complex alpha Subunits Adaptor Proteins, Signal Transducing Adaptor Proteins, Vesicular Transport Amino Acid Sequence Amino acids Antibodies Calcium-Binding Proteins - chemistry Calcium-Binding Proteins - genetics Calcium-Binding Proteins - metabolism Carrier Proteins - chemistry Carrier Proteins - genetics Carrier Proteins - metabolism Cell biology Cell lines Cell Membrane - chemistry Cell Membrane - metabolism Cell membranes Cells Cytosol - metabolism Drosophila Proteins Endocytosis Endosomes - chemistry Endosomes - metabolism Epidermal Growth Factor - metabolism Gene Expression Profiling HeLa cells Humans Intracellular Signaling Peptides and Proteins Membrane Glycoproteins - chemistry Membrane Glycoproteins - metabolism Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - metabolism Membranes Molecular Sequence Data Molecules Nerve Tissue Proteins - chemistry Nerve Tissue Proteins - metabolism Neurons Original Phosphoproteins - chemistry Phosphoproteins - genetics Phosphoproteins - metabolism Plasma Proline - metabolism Protein Binding Protein Structure, Tertiary Protein Subunits Proteins Receptors, LDL - metabolism Sequence Homology, Amino Acid Synaptotagmin II Synaptotagmins Transcription Factors, General Transferrin - metabolism Two-Hybrid System Techniques Vesicular Transport Proteins |
| title | Stonin 2: An Adaptor-like Protein That Interacts with Components of the Endocytic Machinery |
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