A direct interaction with NEDD1 regulates gamma-tubulin recruitment to the centrosome.
The centrosome is the primary microtubule organizing centre of the cell. gamma-tubulin is a core component of the centrosome and is required for microtubule nucleation and centrosome function. The recruitment of gamma-tubulin to centrosomes is mediated by its interaction with NEDD1, a WD40-repeat co...
Main Authors: | , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2010-03-01
|
Series: | PLoS ONE |
Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20224777/?tool=EBI |
id |
doaj-e174ca829aea4650b3b5f46d34295a8a |
---|---|
record_format |
Article |
spelling |
doaj-e174ca829aea4650b3b5f46d34295a8a2021-03-04T12:30:46ZengPublic Library of Science (PLoS)PLoS ONE1932-62032010-03-0153e961810.1371/journal.pone.0009618A direct interaction with NEDD1 regulates gamma-tubulin recruitment to the centrosome.Jantina A ManningSonia ShaliniJoanna M RiskCatherine L DaySharad KumarThe centrosome is the primary microtubule organizing centre of the cell. gamma-tubulin is a core component of the centrosome and is required for microtubule nucleation and centrosome function. The recruitment of gamma-tubulin to centrosomes is mediated by its interaction with NEDD1, a WD40-repeat containing protein. Here we demonstrate that NEDD1 is likely to be oligomeric in vivo and binds directly to gamma-tubulin through a small region of just 62 residues at the carboxyl-terminus of the protein. This carboxyl-terminal domain that binds gamma-tubulin has a helical structure and is a stable tetramer in solution. Mutation of residues in NEDD1 that disrupt binding to gamma-tubulin result in a mis-localization of gamma-tubulin away from the centrosome. Hence, this study defines the binding site on NEDD1 that is required for its interaction with gamma-tubulin, and shows that this interaction is required for the correct localization of gamma-tubulin.https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20224777/?tool=EBI |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Jantina A Manning Sonia Shalini Joanna M Risk Catherine L Day Sharad Kumar |
spellingShingle |
Jantina A Manning Sonia Shalini Joanna M Risk Catherine L Day Sharad Kumar A direct interaction with NEDD1 regulates gamma-tubulin recruitment to the centrosome. PLoS ONE |
author_facet |
Jantina A Manning Sonia Shalini Joanna M Risk Catherine L Day Sharad Kumar |
author_sort |
Jantina A Manning |
title |
A direct interaction with NEDD1 regulates gamma-tubulin recruitment to the centrosome. |
title_short |
A direct interaction with NEDD1 regulates gamma-tubulin recruitment to the centrosome. |
title_full |
A direct interaction with NEDD1 regulates gamma-tubulin recruitment to the centrosome. |
title_fullStr |
A direct interaction with NEDD1 regulates gamma-tubulin recruitment to the centrosome. |
title_full_unstemmed |
A direct interaction with NEDD1 regulates gamma-tubulin recruitment to the centrosome. |
title_sort |
direct interaction with nedd1 regulates gamma-tubulin recruitment to the centrosome. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2010-03-01 |
description |
The centrosome is the primary microtubule organizing centre of the cell. gamma-tubulin is a core component of the centrosome and is required for microtubule nucleation and centrosome function. The recruitment of gamma-tubulin to centrosomes is mediated by its interaction with NEDD1, a WD40-repeat containing protein. Here we demonstrate that NEDD1 is likely to be oligomeric in vivo and binds directly to gamma-tubulin through a small region of just 62 residues at the carboxyl-terminus of the protein. This carboxyl-terminal domain that binds gamma-tubulin has a helical structure and is a stable tetramer in solution. Mutation of residues in NEDD1 that disrupt binding to gamma-tubulin result in a mis-localization of gamma-tubulin away from the centrosome. Hence, this study defines the binding site on NEDD1 that is required for its interaction with gamma-tubulin, and shows that this interaction is required for the correct localization of gamma-tubulin. |
url |
https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20224777/?tool=EBI |
work_keys_str_mv |
AT jantinaamanning adirectinteractionwithnedd1regulatesgammatubulinrecruitmenttothecentrosome AT soniashalini adirectinteractionwithnedd1regulatesgammatubulinrecruitmenttothecentrosome AT joannamrisk adirectinteractionwithnedd1regulatesgammatubulinrecruitmenttothecentrosome AT catherinelday adirectinteractionwithnedd1regulatesgammatubulinrecruitmenttothecentrosome AT sharadkumar adirectinteractionwithnedd1regulatesgammatubulinrecruitmenttothecentrosome AT jantinaamanning directinteractionwithnedd1regulatesgammatubulinrecruitmenttothecentrosome AT soniashalini directinteractionwithnedd1regulatesgammatubulinrecruitmenttothecentrosome AT joannamrisk directinteractionwithnedd1regulatesgammatubulinrecruitmenttothecentrosome AT catherinelday directinteractionwithnedd1regulatesgammatubulinrecruitmenttothecentrosome AT sharadkumar directinteractionwithnedd1regulatesgammatubulinrecruitmenttothecentrosome |
_version_ |
1714802434655649792 |