TD-60 links RalA GTPase function to the CPC in mitosis

Diana Papini, Lars Langemeyer, Maria A. Abad, Alastair Kerr, Itaru Samejima, Patrick A. Eyers, A. Arockia Jeyaprakash, Jonathan M. G. Higgins (), Francis A. Barr and William C. Earnshaw ()
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Diana Papini: Wellcome Trust Centre for Cell Biology, Institute of Cell Biology, University of Edinburgh
Lars Langemeyer: University of Oxford
Maria A. Abad: Wellcome Trust Centre for Cell Biology, Institute of Cell Biology, University of Edinburgh
Alastair Kerr: Wellcome Trust Centre for Cell Biology, Institute of Cell Biology, University of Edinburgh
Itaru Samejima: Wellcome Trust Centre for Cell Biology, Institute of Cell Biology, University of Edinburgh
Patrick A. Eyers: Institute of Integrative Biology, University of Liverpool
A. Arockia Jeyaprakash: Wellcome Trust Centre for Cell Biology, Institute of Cell Biology, University of Edinburgh
Jonathan M. G. Higgins: Institute for Cell and Molecular Biosciences (ICaMB), Newcastle University, Medical School
Francis A. Barr: University of Oxford
William C. Earnshaw: Wellcome Trust Centre for Cell Biology, Institute of Cell Biology, University of Edinburgh

Nature Communications, 2015, vol. 6, issue 1, 1-12

Abstract: Abstract TD-60 (also known as RCC2) is a highly conserved protein that structurally resembles the Ran guanine exchange factor (GEF) RCC1, but has not previously been shown to have GEF activity. TD-60 has a typical chromosomal passenger complex (CPC) distribution in mitotic cells, but associates with integrin complexes and is involved in cell motility during interphase. Here we show that TD-60 exhibits GEF activity, in vitro and in cells, for the small GTPase RalA. TD-60 or RalA depletion causes spindle abnormalities in prometaphase associated with abnormal centromeric accumulation of CPC components. TD-60 and RalA apparently work together to contribute to the regulation of kinetochore–microtubule interactions in early mitosis. Importantly, several mitotic phenotypes caused by TD-60 depletion are reverted by the expression of a GTP-locked mutant, RalA (Q72L). The demonstration that a small GTPase participates in the regulation of the CPC reveals a level of mitotic regulation not suspected in previous studies.

Date: 2015
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DOI: 10.1038/ncomms8678

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