Intracellular membrane trafficking requires the complex interplay of several classes of trafficking proteins. Rab proteins, the largest subfamily of the Ras superfamily of small G-proteins, are central regulators of all aspects of intracellular trafficking processes including vesicle budding and uncoating, motility, tethering and fusion. In the present paper, we discuss the discovery, evolution and characterization of the Rab GTPase family. We examine their basic functional roles, their important structural features and the regulatory proteins which mediate Rab function. We speculate on outstanding issues in the field, such as the mechanisms of Rab membrane association and the co-ordinated interplay between distinct Rab proteins. Finally, we summarize the data implicating Rab proteins in an ever increasing number of diseases.
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December 2012
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Conference Article|
November 21 2012
The Rab family of proteins: 25 years on
Eoin E. Kelly;
Eoin E. Kelly
*Molecular Cell Biology Laboratory, Department of Biochemistry, BioSciences Institute, University College Cork, Cork, Ireland
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Conor P. Horgan;
Conor P. Horgan
*Molecular Cell Biology Laboratory, Department of Biochemistry, BioSciences Institute, University College Cork, Cork, Ireland
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Bruno Goud;
Bruno Goud
†Unité Mixte de Recherche 144, Centre National de la Recherche Scientifique, Institut Curie, Laboratory Molecular Mechanisms of Intracellular Transport, Paris, France
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Mary W. McCaffrey
Mary W. McCaffrey
1
*Molecular Cell Biology Laboratory, Department of Biochemistry, BioSciences Institute, University College Cork, Cork, Ireland
1To whom correspondence should be addressed (emailm.mccaffrey@ucc.ie).
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Publisher: Portland Press Ltd
Received:
August 14 2012
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2012 The Authors Journal
2012
Biochem Soc Trans (2012) 40 (6): 1337–1347.
Article history
Received:
August 14 2012
Citation
Eoin E. Kelly, Conor P. Horgan, Bruno Goud, Mary W. McCaffrey; The Rab family of proteins: 25 years on. Biochem Soc Trans 1 December 2012; 40 (6): 1337–1347. doi: https://doi.org/10.1042/BST20120203
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