The nuclear localization of γ-tubulin is regulated by SadB-mediated phosphorylation.

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Bibtex

@article{be7e1e0879b54a40b91407fa19b67f1c,
title = "The nuclear localization of γ-tubulin is regulated by SadB-mediated phosphorylation.",
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 = "Greta Eklund and Stefan Lang and Johan Glindre and {\AA}sa Ehl{\'e}n and Maria Alvarado-Kristensson",
year = "2014",
doi = "10.1074/jbc.M114.562389",
language = "English",
volume = "289",
pages = "21360--21373",
journal = "Journal of Biological Chemistry",
issn = "1083-351X",
publisher = "ASBMB",
number = "31",

}