Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors
A key requirement for Rab function in membrane trafficking is site-specific activation by GDP-GTP exchange factors (GEFs), but the majority of the 63 human Rabs have no known GEF. We have performed a systematic characterization of the 17 human DENN domain proteins and demonstrated that they are spec...
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| Veröffentlicht in: | The Journal of cell biology 2010-10, Vol.191 (2), p.367-381 |
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| container_title | The Journal of cell biology |
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| creator | Yoshimura, Shin-ichiro Gerondopoulos, Andreas Linford, Andrea Rigden, Daniel J Barr, Francis A |
| description | A key requirement for Rab function in membrane trafficking is site-specific activation by GDP-GTP exchange factors (GEFs), but the majority of the 63 human Rabs have no known GEF. We have performed a systematic characterization of the 17 human DENN domain proteins and demonstrated that they are specific GEFs for 10 Rabs. DENND1A/1B localize to clathrin patches at the plasma membrane and activate Rab35 in an endocytic pathway trafficking Shiga toxin to the trans-Golgi network. DENND2 GEFs target to actin filaments and control Rab9-dependent trafficking of mannose-6-phosphate receptor to lysosomes. DENND4 GEFs target to a tubular membrane compartment adjacent to the Golgi, where they activate Rab10, which suggests a function in basolateral polarized sorting in epithelial cells that compliments the non-DENN GEF Sec2 acting on Rab8 in apical sorting. DENND1C, DENND3, DENND5A/5B, MTMR5/13, and MADD activate Rab13, Rab12, Rab39, Rab28, and Rab27A/27B, respectively. Together, these findings provide a basis for future studies on Rab regulation and function. |
| doi_str_mv | 10.1083/jcb.201008051 |
| format | Article |
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We have performed a systematic characterization of the 17 human DENN domain proteins and demonstrated that they are specific GEFs for 10 Rabs. DENND1A/1B localize to clathrin patches at the plasma membrane and activate Rab35 in an endocytic pathway trafficking Shiga toxin to the trans-Golgi network. DENND2 GEFs target to actin filaments and control Rab9-dependent trafficking of mannose-6-phosphate receptor to lysosomes. DENND4 GEFs target to a tubular membrane compartment adjacent to the Golgi, where they activate Rab10, which suggests a function in basolateral polarized sorting in epithelial cells that compliments the non-DENN GEF Sec2 acting on Rab8 in apical sorting. DENND1C, DENND3, DENND5A/5B, MTMR5/13, and MADD activate Rab13, Rab12, Rab39, Rab28, and Rab27A/27B, respectively. Together, these findings provide a basis for future studies on Rab regulation and function.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.201008051</identifier><identifier>PMID: 20937701</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: The Rockefeller University Press</publisher><subject>Antibodies ; Binding sites ; Biological Transport ; Cell membranes ; Cells ; Endosomes ; Epithelial cells ; Guanine Nucleotide Exchange Factors - analysis ; Guanine Nucleotide Exchange Factors - chemistry ; Guanine Nucleotide Exchange Factors - physiology ; HeLa Cells ; Humans ; Kidney cells ; Lysosomes - metabolism ; Membranes ; Physiological regulation ; Protein Structure, Tertiary ; Proteins ; rab GTP-Binding Proteins - analysis ; rab GTP-Binding Proteins - chemistry ; rab GTP-Binding Proteins - physiology ; Recycling ; Shiga Toxin - metabolism ; T cell receptors ; Toxins ; Trans golgi network ; trans-Golgi Network - metabolism</subject><ispartof>The Journal of cell biology, 2010-10, Vol.191 (2), p.367-381</ispartof><rights>Copyright Rockefeller University Press Oct 18, 2010</rights><rights>2010 Yoshimura et al. 2010</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c525t-785d3f6d1b71ecf6d7964a8d3cfa3428c4e842c8ceeea7736a3b6dadfd87739d3</citedby><cites>FETCH-LOGICAL-c525t-785d3f6d1b71ecf6d7964a8d3cfa3428c4e842c8ceeea7736a3b6dadfd87739d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20937701$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yoshimura, Shin-ichiro</creatorcontrib><creatorcontrib>Gerondopoulos, Andreas</creatorcontrib><creatorcontrib>Linford, Andrea</creatorcontrib><creatorcontrib>Rigden, Daniel J</creatorcontrib><creatorcontrib>Barr, Francis A</creatorcontrib><title>Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>A key requirement for Rab function in membrane trafficking is site-specific activation by GDP-GTP exchange factors (GEFs), but the majority of the 63 human Rabs have no known GEF. We have performed a systematic characterization of the 17 human DENN domain proteins and demonstrated that they are specific GEFs for 10 Rabs. DENND1A/1B localize to clathrin patches at the plasma membrane and activate Rab35 in an endocytic pathway trafficking Shiga toxin to the trans-Golgi network. DENND2 GEFs target to actin filaments and control Rab9-dependent trafficking of mannose-6-phosphate receptor to lysosomes. DENND4 GEFs target to a tubular membrane compartment adjacent to the Golgi, where they activate Rab10, which suggests a function in basolateral polarized sorting in epithelial cells that compliments the non-DENN GEF Sec2 acting on Rab8 in apical sorting. DENND1C, DENND3, DENND5A/5B, MTMR5/13, and MADD activate Rab13, Rab12, Rab39, Rab28, and Rab27A/27B, respectively. 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Gerondopoulos, Andreas ; Linford, Andrea ; Rigden, Daniel J ; Barr, Francis A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c525t-785d3f6d1b71ecf6d7964a8d3cfa3428c4e842c8ceeea7736a3b6dadfd87739d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Antibodies</topic><topic>Binding sites</topic><topic>Biological Transport</topic><topic>Cell membranes</topic><topic>Cells</topic><topic>Endosomes</topic><topic>Epithelial cells</topic><topic>Guanine Nucleotide Exchange Factors - analysis</topic><topic>Guanine Nucleotide Exchange Factors - chemistry</topic><topic>Guanine Nucleotide Exchange Factors - physiology</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Kidney cells</topic><topic>Lysosomes - metabolism</topic><topic>Membranes</topic><topic>Physiological regulation</topic><topic>Protein Structure, Tertiary</topic><topic>Proteins</topic><topic>rab GTP-Binding Proteins - analysis</topic><topic>rab GTP-Binding Proteins - chemistry</topic><topic>rab GTP-Binding Proteins - physiology</topic><topic>Recycling</topic><topic>Shiga Toxin - metabolism</topic><topic>T cell receptors</topic><topic>Toxins</topic><topic>Trans golgi network</topic><topic>trans-Golgi Network - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yoshimura, Shin-ichiro</creatorcontrib><creatorcontrib>Gerondopoulos, Andreas</creatorcontrib><creatorcontrib>Linford, Andrea</creatorcontrib><creatorcontrib>Rigden, Daniel J</creatorcontrib><creatorcontrib>Barr, Francis A</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</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>Yoshimura, Shin-ichiro</au><au>Gerondopoulos, Andreas</au><au>Linford, Andrea</au><au>Rigden, Daniel J</au><au>Barr, Francis A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>2010-10-18</date><risdate>2010</risdate><volume>191</volume><issue>2</issue><spage>367</spage><epage>381</epage><pages>367-381</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>A key requirement for Rab function in membrane trafficking is site-specific activation by GDP-GTP exchange factors (GEFs), but the majority of the 63 human Rabs have no known GEF. We have performed a systematic characterization of the 17 human DENN domain proteins and demonstrated that they are specific GEFs for 10 Rabs. DENND1A/1B localize to clathrin patches at the plasma membrane and activate Rab35 in an endocytic pathway trafficking Shiga toxin to the trans-Golgi network. DENND2 GEFs target to actin filaments and control Rab9-dependent trafficking of mannose-6-phosphate receptor to lysosomes. DENND4 GEFs target to a tubular membrane compartment adjacent to the Golgi, where they activate Rab10, which suggests a function in basolateral polarized sorting in epithelial cells that compliments the non-DENN GEF Sec2 acting on Rab8 in apical sorting. DENND1C, DENND3, DENND5A/5B, MTMR5/13, and MADD activate Rab13, Rab12, Rab39, Rab28, and Rab27A/27B, respectively. Together, these findings provide a basis for future studies on Rab regulation and function.</abstract><cop>United States</cop><pub>The Rockefeller University Press</pub><pmid>20937701</pmid><doi>10.1083/jcb.201008051</doi><tpages>15</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Antibodies Binding sites Biological Transport Cell membranes Cells Endosomes Epithelial cells Guanine Nucleotide Exchange Factors - analysis Guanine Nucleotide Exchange Factors - chemistry Guanine Nucleotide Exchange Factors - physiology HeLa Cells Humans Kidney cells Lysosomes - metabolism Membranes Physiological regulation Protein Structure, Tertiary Proteins rab GTP-Binding Proteins - analysis rab GTP-Binding Proteins - chemistry rab GTP-Binding Proteins - physiology Recycling Shiga Toxin - metabolism T cell receptors Toxins Trans golgi network trans-Golgi Network - metabolism |
| title | Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors |
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