Premium
Does Rho Inhibition Alter Microtubule Acetylation and Detyrosination?
Author(s) -
McGee James P,
Danowski Barbara A
Publication year - 2016
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.30.1_supplement.1226.1
Subject(s) - microtubule , acetylation , microbiology and biotechnology , cytoskeleton , tubulin , actin , crosstalk , contractility , myosin , chemistry , biology , cell , biochemistry , gene , physics , endocrinology , optics
Microtubules (MTs) play a role in many cellular functions, such as chromosome segregation, establishment of polarity, and vesicle transport. Numerous post‐translational modifications (PTMs) to tubulin have been identified, but their functions are still not well‐understood. Microtubules are also known to modulate actin‐based cell contractility; changes in MT dynamics have been shown to play a role in this crosstalk. Actin‐myosin contractility is mediated through rho, a member of the Rho family of GTPases. Prior studies have shown a possible relationship between increased contractility due to rho activation and specific tubulin post‐translational modifications. In order to investigate this further, we examined whether the amount and/or localization of acetylated and detyrosinated MTs changes when rho is inhibited. Immunofluorescence was performed on C3H10T1/2 mouse embryo fibroblasts that were treated with a membrane‐permeant rho inhibitor for 1 & 4 hours and evaluated for alpha‐tubulin and either detyrosinated or acetylated tubulin. Cells were scored based on the presence of high, medium or low amounts of each of the post‐translational modifications. Based on 3 separate experiments, we found a statistically significant decrease in the amount of acetylated MTs but no difference in detyrosinated MTs. Western blotting will be done to determine whether rho inhibition alters the concentrations of the modified tubulins in cell extracts. These results could shed further light on the mechanisms of microtubule‐actin cytoskeletal crosstalk and provide insight into the role of acetylated microtubules.