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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)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
289
issue
31
pages
21360 - 21373
publisher
ASBMB
external identifiers
  • pmid:24942739
  • wos:000340558300016
  • scopus:84905387200
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
2014-07-06 13:12:48
date last changed
2017-01-01 03:48:19
@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    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {The nuclear localization of γ-tubulin is regulated by SadB-mediated phosphorylation.},
  url          = {http://dx.doi.org/10.1074/jbc.M114.562389},
  volume       = {289},
  year         = {2014},
}