The nuclear localization of γ-tubulin is regulated by SadB-mediated phosphorylation.
Eklund, Greta LU ; Lang, Stefan LU
; Glindre, Johan
LU
; Ehlén, Åsa
LU
and Alvarado-Kristensson, Maria
LU
(2014)
In Journal of Biological Chemistry
289(31).
p.21360-21373
- Abstract
- γ-tubulin is an important cell division regulator that arranges microtubule assembly and mitotic spindle formation. Cytosolic γ-tubulin nucleates α- and β-tubulin in a growing microtubule by forming the ring-shaped protein complex γTuRC. Nuclear γ-tubulin also regulates S-phase progression by moderating the activities of E2Fs. The mechanism that regulates localization of γ-tubulin is currently unknown. Here, we describe that the human Ser/Thr kinase SadB short localizes to chromatin and centrosomes. We found that SadB-mediated phosphorylation of γ-tubulin on Ser 385 triggered formation of chromatin associated γ-tubulin complexes that moderates gene expression. In this way, the C terminal region of γ-tubulin regulates S-phase progression.... (More)
- γ-tubulin is an important cell division regulator that arranges microtubule assembly and mitotic spindle formation. Cytosolic γ-tubulin nucleates α- and β-tubulin in a growing microtubule by forming the ring-shaped protein complex γTuRC. Nuclear γ-tubulin also regulates S-phase progression by moderating the activities of E2Fs. The mechanism that regulates localization of γ-tubulin is currently unknown. Here, we describe that the human Ser/Thr kinase SadB short localizes to chromatin and centrosomes. We found that SadB-mediated phosphorylation of γ-tubulin on Ser 385 triggered formation of chromatin associated γ-tubulin complexes that moderates gene expression. In this way, the C terminal region of γ-tubulin regulates S-phase progression. In addition, chromatin levels of γ-tubulin were decreased by reduction of SadB levels or expression of a non-phosphorylatable Ala-385-γ-tubulin, but were enhanced by expression of SadB, wild-type γ-tubulin, or a phosphomimetic Asp-385-γ-tubulin mutant. Our results demonstrate that SadB kinases regulate the cellular localization of γ-tubulin and thereby control S-phase progression. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4528198
- author
- Eklund, Greta
LU
; Lang, Stefan
LU
; Glindre, Johan
LU
; Ehlén, Åsa
LU
and Alvarado-Kristensson, Maria
LU
- organization
- publishing date
- 2014
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 289
- issue
- 31
- pages
- 21360 - 21373
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- pmid:24942739
- wos:000340558300016
- scopus:84905387200
- pmid:24942739
- ISSN
- 1083-351X
- DOI
- 10.1074/jbc.M114.562389
- language
- English
- LU publication?
- yes
- id
- be7e1e08-79b5-4a40-b914-07fa19b67f1c (old id 4528198)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/24942739?dopt=Abstract
- date added to LUP
- 2016-04-01 10:40:49
- date last changed
- 2025-10-14 09:59:18
@article{be7e1e08-79b5-4a40-b914-07fa19b67f1c,
abstract = {{γ-tubulin is an important cell division regulator that arranges microtubule assembly and mitotic spindle formation. Cytosolic γ-tubulin nucleates α- and β-tubulin in a growing microtubule by forming the ring-shaped protein complex γTuRC. Nuclear γ-tubulin also regulates S-phase progression by moderating the activities of E2Fs. The mechanism that regulates localization of γ-tubulin is currently unknown. Here, we describe that the human Ser/Thr kinase SadB short localizes to chromatin and centrosomes. We found that SadB-mediated phosphorylation of γ-tubulin on Ser 385 triggered formation of chromatin associated γ-tubulin complexes that moderates gene expression. In this way, the C terminal region of γ-tubulin regulates S-phase progression. In addition, chromatin levels of γ-tubulin were decreased by reduction of SadB levels or expression of a non-phosphorylatable Ala-385-γ-tubulin, but were enhanced by expression of SadB, wild-type γ-tubulin, or a phosphomimetic Asp-385-γ-tubulin mutant. Our results demonstrate that SadB kinases regulate the cellular localization of γ-tubulin and thereby control S-phase progression.}},
author = {{Eklund, Greta and Lang, Stefan and Glindre, Johan and Ehlén, Åsa and Alvarado-Kristensson, Maria}},
issn = {{1083-351X}},
language = {{eng}},
number = {{31}},
pages = {{21360--21373}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Journal of Biological Chemistry}},
title = {{The nuclear localization of γ-tubulin is regulated by SadB-mediated phosphorylation.}},
url = {{https://lup.lub.lu.se/search/files/2047500/5268134}},
doi = {{10.1074/jbc.M114.562389}},
volume = {{289}},
year = {{2014}},
}