Literature DB >> 7613510

Acetylation of alpha-tubilin in different bovine cell types: implications for microtubule dynamics in interphase and mitosis.

K W Wolf1, K Spanel-Borowski.   

Abstract

Previous work on five cell types isolated from the bovine corpus luteum showed that the mass of acetylated microtubules (acet-MTs) in interphase differed. Endothelial cells, termed type 3, showed few acet-MTs, whereas the interphase cytoskeleton of granulosal-like cells, termed type 5, was rich in acet-MTs. In the present study, these cultured cells were used to determine whether the degree of alpha-tubulin acetylation in interphase had consequences on mitosis. To this end, the distribution of acet-MTs was determined throughout the cell cycle using a monoclonal antibody, 6-11B-1, directed against acetylated alpha-tubulin. For comparison, tyrosinated MTs were visualized with another monoclonal antibody, YL1/2, detecting tyrosinated alpha-tubulin. Although the amount of acet-MTs in interphase differed significantly between both cell types, major differences in the appearance of acet-MTs during mitosis were only apparent in prophase and during transition from late telophase to interphase. Thus, irrespective of different alpha-tubulin acetylation in interphase, spindle structure is uniform. Since acetylation of alpha-tubulin is believed to indicate the presence of relatively stable MTs, we conclude that MT dynamics is differently controlled in interphase and mitosis. Thereby interphase cells are able to carry out functions which involve stable MTs and the cells progress through mitosis in the presence of more dynamic MTs.

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Year:  1995        PMID: 7613510     DOI: 10.1006/cbir.1995.1006

Source DB:  PubMed          Journal:  Cell Biol Int        ISSN: 1065-6995            Impact factor:   3.612


  2 in total

1.  Estimating microtubule distributions from 2D immunofluorescence microscopy images reveals differences among human cultured cell lines.

Authors:  Jieyue Li; Aabid Shariff; Mikaela Wiking; Emma Lundberg; Gustavo K Rohde; Robert F Murphy
Journal:  PLoS One       Date:  2012-11-28       Impact factor: 3.240

2.  Mutations in SIRT2 deacetylase which regulate enzymatic activity but not its interaction with HDAC6 and tubulin.

Authors:  Fatimah Nahhas; Sylvia C Dryden; Judith Abrams; Michael A Tainsky
Journal:  Mol Cell Biochem       Date:  2007-05-22       Impact factor: 3.842

  2 in total

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