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...
Bewaard in:
Hoofdauteurs: | , , , , , , , , , |
---|---|
Formaat: | Artigo |
Taal: | Engels |
Gepubliceerd in: |
2015
|
Online toegang: | https://doi.org/10.1038/ncomms8678 https://www.nature.com/articles/ncomms8678.pdf |
Tags: |
Voeg label toe
Geen labels, Wees de eerste die dit record labelt!
|
_version_ | 1838900870139346944 |
---|---|
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 |