Structural Basis for Recruitment of Rab6-Interacting Protein 1 to Golgi via a RUN Domain
| Autor: | Florence Jollivet, Solange Monier, Bruno Goud, Anne Houdusse, Amir R. Khan, Annick Boulet, Rosario Recacha |
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| Přispěvatelé: | School of Biochemistry and Immunology, Trinity College Dublin, Compartimentation et dynamique cellulaires (CDC), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut Curie [Paris]-Centre National de la Recherche Scientifique (CNRS), Institut de Génétique et Développement de Rennes (IGDR), Université de Rennes (UR)-Centre National de la Recherche Scientifique (CNRS), Institut de biologie et chimie des protéines [Lyon] (IBCP), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), De Villemeur, Hervé, Centre National de la Recherche Scientifique (CNRS)-Institut Curie [Paris]-Université Pierre et Marie Curie - Paris 6 (UPMC), Centre National de la Recherche Scientifique (CNRS)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES) |
| Jazyk: | angličtina |
| Rok vydání: | 2009 |
| Předmět: |
PLAT domain
Models Molecular PROTEINS Protein Conformation Golgi Apparatus [SDV.BC]Life Sciences [q-bio]/Cellular Biology RUN domain Biology 03 medical and health sciences symbols.namesake Protein structure RAB6A Structural Biology Two-Hybrid System Techniques Small GTPase Molecular Biology [SDV.BC] Life Sciences [q-bio]/Cellular Biology 030304 developmental biology Adaptor Proteins Signal Transducing DNA Primers Genetics 0303 health sciences Base Sequence Effector 030302 biochemistry & molecular biology Golgi apparatus Cell biology symbols CELLBIO Alpha helix |
| Zdroj: | Structure / Struct Fold Des; Structure (Camb ) Structure / Struct Fold Des; Structure (Camb ), 2009, 17 (1), pp.21-30. ⟨10.1016/j.str.2008.10.014⟩ |
| Popis: | International audience; Small GTPase Rab6 regulates vesicle trafficking at the level of Golgi via recruitment of numerous and unrelated effectors. The crystal structure of Rab6a(GTP) in complex with a 378-residue internal fragment of the effector Rab6IP1 was solved at 3.2 A resolution. This Rab6IP1 region encompasses an all alpha-helical RUN domain followed in tandem by a PLAT domain that adopts a beta sandwich fold. The structure reveals that the first and last alpha helices of the RUN domain mediate binding to switch I, switch II, and the interswitch region of Rab6. It represents the largest Rab-effector complex determined to date. Comparisons with the recent structure of Rab6 in complex with an unrelated effector, human golgin GCC185, reveals significant conformational changes in the conserved hydrophobic triad of Rab6. Flexibility in the switch and interswitch regions of Rab6 mediates recognition of compositionally distinct alpha-helical coiled coils, thereby contributing to Rab6 promiscuity in effector recruitment. |
| Databáze: | OpenAIRE |
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