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Merck
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Cep70 regulates microtubule stability by interacting with HDAC6.

FEBS letters (2015-06-27)
Xingjuan Shi, Yanjun Yao, Yujue Wang, Yu Zhang, Qinghai Huang, Jun Zhou, Min Liu, Dengwen Li
ABSTRACT

Microtubules, highly dynamic components of the cytoskeleton, are involved in mitosis, cell migration and intracellular trafficking. Our previous work has shown that the centrosomal protein Cep70 regulates microtubule organization and mitotic spindle orientation in mammalian cells. However, it remains elusive whether Cep70 is implicated in microtubule stability. Here we demonstrate that Cep70 enhances microtubule resistance to cold or nocodazole treatment. Our data further show that Cep70 promotes microtubule stability by regulating tubulin acetylation, and plays an important role in stabilizing microtubules. Mechanistic studies reveal that Cep70 interacts and colocalizes with histone deacetylase 6 (HDAC6) in the cytoplasm. These findings suggest that Cep70 promotes microtubule stability by interaction with HDAC6 and regulation of tubulin acetylation.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Anti-Acetylated Tubulin antibody, Mouse monoclonal, clone 6-11B-1, purified from hybridoma cell culture
Sigma-Aldrich
Nocodazole, ≥99% (TLC), powder
Sigma-Aldrich
DAPI, for nucleic acid staining
Sigma-Aldrich
L-Glutathione reduced, suitable for cell culture, BioReagent, ≥98.0%, powder
Sigma-Aldrich
L-Glutathione reduced, Vetec, reagent grade, ≥98%
Sigma-Aldrich
L-Glutathione reduced, BioXtra, ≥98.0%
Sigma-Aldrich
L-Glutathione reduced, ≥98.0%