The small GTPase Rab6 regulates vesicle trafficking at the level of Golgi. Recently, the crystal structures of Rab6 in complexes with two unrelated effectors have been determined. The structure of Rab6a-GTP in complex with a 378-residue internal fragment of the effector Rab6IP1 (Rab6-interacting protein 1) has been solved. In addition, the structure of Rab6 with the golgin, GCC185, has also been determined. In both complexes, two α-helices from the effector mediate binding to switch I, switch II and the interswitch region of Rab6. Comparisons of the complexes reveal significant conformational changes in the conserved hydrophobic triad of Rab6. Thus conformational flexibility in the triad mediates recognition of compositionally distinct α-helical coiled coils, providing a rationale for the promiscuity of Rab6 in effector recruitment.
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October 2009
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Conference Article|
September 21 2009
Structural aspects of Rab6–effector complexes
Humberto Fernandes;
Humberto Fernandes
1
*School of Biochemistry and Immunology, Trinity College, Dublin 2, Ireland
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Edward Franklin;
Edward Franklin
1
*School of Biochemistry and Immunology, Trinity College, Dublin 2, Ireland
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Rosario Recacha;
Rosario Recacha
*School of Biochemistry and Immunology, Trinity College, Dublin 2, Ireland
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Anne Houdusse;
Anne Houdusse
†UMR 144 CNRS/Institut Curie, Institut Curie, Paris 75005, France
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Bruno Goud;
Bruno Goud
†UMR 144 CNRS/Institut Curie, Institut Curie, Paris 75005, France
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Amir R. Khan
Amir R. Khan
2
*School of Biochemistry and Immunology, Trinity College, Dublin 2, Ireland
2To whom correspondence should be addressed (email amirrafk@tcd.ie).
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Publisher: Portland Press Ltd
Received:
April 22 2009
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2009 Biochemical Society
2009
Biochem Soc Trans (2009) 37 (5): 1037–1041.
Article history
Received:
April 22 2009
Citation
Humberto Fernandes, Edward Franklin, Rosario Recacha, Anne Houdusse, Bruno Goud, Amir R. Khan; Structural aspects of Rab6–effector complexes. Biochem Soc Trans 1 October 2009; 37 (5): 1037–1041. doi: https://doi.org/10.1042/BST0371037
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