Multiple Rab GTPase binding sites in GCC185 suggest a model for vesicle tethering at the trans-Golgi
GCC185, a trans-Golgi network-localized protein predicted to assume a long, coiled-coil structure, is required for Rab9-dependent recycling of mannose 6-phosphate receptors (MPRs) to the Golgi and for microtubule nucleation at the Golgi via CLASP proteins. GCC185 localizes to the Golgi by cooperativ...
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Published in | Molecular biology of the cell Vol. 20; no. 1; pp. 209 - 217 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
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The American Society for Cell Biology
01.01.2009
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Abstract | GCC185, a trans-Golgi network-localized protein predicted to assume a long, coiled-coil structure, is required for Rab9-dependent recycling of mannose 6-phosphate receptors (MPRs) to the Golgi and for microtubule nucleation at the Golgi via CLASP proteins. GCC185 localizes to the Golgi by cooperative interaction with Rab6 and Arl1 GTPases at adjacent sites near its C terminus. We show here by yeast two-hybrid and direct biochemical tests that GCC185 contains at least four additional binding sites for as many as 14 different Rab GTPases across its entire length. A central coiled-coil domain contains a specific Rab9 binding site, and functional assays indicate that this domain is important for MPR recycling to the Golgi complex. N-Terminal coiled-coils are also required for GCC185 function as determined by plasmid rescue after GCC185 depletion by using small interfering RNA in cultured cells. Golgi-Rab binding sites may permit GCC185 to contribute to stacking and lateral interactions of Golgi cisternae as well as help it function as a vesicle tether. |
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AbstractList | GCC185, a trans-Golgi network-localized protein predicted to assume a long, coiled-coil structure, is required for Rab9-dependent recycling of mannose 6-phosphate receptors (MPRs) to the Golgi and for microtubule nucleation at the Golgi via CLASP proteins. GCC185 localizes to the Golgi by cooperative interaction with Rab6 and Arl1 GTPases at adjacent sites near its C terminus. We show here by yeast two-hybrid and direct biochemical tests that GCC185 contains at least four additional binding sites for as many as 14 different Rab GTPases across its entire length. A central coiled-coil domain contains a specific Rab9 binding site, and functional assays indicate that this domain is important for MPR recycling to the Golgi complex. N-Terminal coiled-coils are also required for GCC185 function as determined by plasmid rescue after GCC185 depletion by using small interfering RNA in cultured cells. Golgi-Rab binding sites may permit GCC185 to contribute to stacking and lateral interactions of Golgi cisternae as well as help it function as a vesicle tether. GCC185, a trans -Golgi network-localized protein predicted to assume a long, coiled-coil structure, is required for Rab9-dependent recycling of mannose 6-phosphate receptors (MPRs) to the Golgi and for microtubule nucleation at the Golgi via CLASP proteins. GCC185 localizes to the Golgi by cooperative interaction with Rab6 and Arl1 GTPases at adjacent sites near its C terminus. We show here by yeast two-hybrid and direct biochemical tests that GCC185 contains at least four additional binding sites for as many as 14 different Rab GTPases across its entire length. A central coiled-coil domain contains a specific Rab9 binding site, and functional assays indicate that this domain is important for MPR recycling to the Golgi complex. N-Terminal coiled-coils are also required for GCC185 function as determined by plasmid rescue after GCC185 depletion by using small interfering RNA in cultured cells. Golgi-Rab binding sites may permit GCC185 to contribute to stacking and lateral interactions of Golgi cisternae as well as help it function as a vesicle tether. |
Author | Brown, Frank C Pfeffer, Suzanne R Nottingham, Ryan M Haas, Alexander K Hayes, Garret L Barr, Francis A |
Author_xml | – sequence: 1 givenname: Garret L surname: Hayes fullname: Hayes, Garret L organization: Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305, USA – sequence: 2 givenname: Frank C surname: Brown fullname: Brown, Frank C – sequence: 3 givenname: Alexander K surname: Haas fullname: Haas, Alexander K – sequence: 4 givenname: Ryan M surname: Nottingham fullname: Nottingham, Ryan M – sequence: 5 givenname: Francis A surname: Barr fullname: Barr, Francis A – sequence: 6 givenname: Suzanne R surname: Pfeffer fullname: Pfeffer, Suzanne R |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/18946081$$D View this record in MEDLINE/PubMed |
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Snippet | GCC185, a trans-Golgi network-localized protein predicted to assume a long, coiled-coil structure, is required for Rab9-dependent recycling of mannose... GCC185, a trans -Golgi network-localized protein predicted to assume a long, coiled-coil structure, is required for Rab9-dependent recycling of mannose... |
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StartPage | 209 |
SubjectTerms | ADP-Ribosylation Factors - genetics ADP-Ribosylation Factors - metabolism Binding Sites Cytoplasmic Vesicles - metabolism Golgi Apparatus - metabolism Golgi Apparatus - ultrastructure Golgi Matrix Proteins HeLa Cells Humans Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - metabolism Protein Isoforms - genetics Protein Isoforms - metabolism rab GTP-Binding Proteins - genetics rab GTP-Binding Proteins - metabolism trans-Golgi Network - metabolism trans-Golgi Network - ultrastructure Two-Hybrid System Techniques |
Title | Multiple Rab GTPase binding sites in GCC185 suggest a model for vesicle tethering at the trans-Golgi |
URI | https://www.ncbi.nlm.nih.gov/pubmed/18946081 https://search.proquest.com/docview/66784039 https://pubmed.ncbi.nlm.nih.gov/PMC2613123 |
Volume | 20 |
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