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

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...

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Hoofdauteurs: Diana Papini, Lars Langemeyer, Maria Alba Abad, Alastair Kerr, Itaru Samejima, Patrick A. Eyers, A. Arockia Jeyaprakash, Jonathan M.G. Higgins, Francis A. Barr, William C. Earnshaw
Formaat: Artigo
Taal:Engels
Gepubliceerd in: 2015
Online toegang:https://doi.org/10.1038/ncomms8678
https://www.nature.com/articles/ncomms8678.pdf
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access_facet Acesso Aberto
author Diana Papini
Lars Langemeyer
Maria Alba Abad
Alastair Kerr
Itaru Samejima
Patrick A. Eyers
A. Arockia Jeyaprakash
Jonathan M.G. Higgins
Francis A. Barr
William C. Earnshaw
author_facet Diana Papini
Lars Langemeyer
Maria Alba Abad
Alastair Kerr
Itaru Samejima
Patrick A. Eyers
A. Arockia Jeyaprakash
Jonathan M.G. Higgins
Francis A. Barr
William C. Earnshaw
cited_by_count_is 52
collection OpenAlex
description 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.
format Artigo
frbr_group_id_str doi-10.1038/ncomms8678
id openalex-W646763754
institution Wellcome Centre for Cell Biology
issn_str 2041-1723
issue_str 1
journal_title_str Nature Communications
language eng
publishDate 2015
publisher_str Nature Portfolio
spellingShingle TD-60 links RalA GTPase function to the CPC in mitosis
Diana Papini
Lars Langemeyer
Maria Alba Abad
Alastair Kerr
Itaru Samejima
Patrick A. Eyers
A. Arockia Jeyaprakash
Jonathan M.G. Higgins
Francis A. Barr
William C. Earnshaw
title TD-60 links RalA GTPase function to the CPC in mitosis
title_full TD-60 links RalA GTPase function to the CPC in mitosis
title_fullStr TD-60 links RalA GTPase function to the CPC in mitosis
title_full_unstemmed TD-60 links RalA GTPase function to the CPC in mitosis
title_short TD-60 links RalA GTPase function to the CPC in mitosis
topic_facet Mitosis
Cell biology
Prometaphase
GTPase
Ran
Guanine nucleotide exchange factor
Small GTPase
Biology
Mitotic exit
Kinetochore
Interphase
Cell cycle
Spindle apparatus
Cell division
Cell
Genetics
Anaphase
Signal transduction
Gene
Chromosome
url https://doi.org/10.1038/ncomms8678
https://www.nature.com/articles/ncomms8678.pdf
volume_str 6