Results 41 to 50 of about 21,416 (200)

RASSF1A Regulates Spindle Organization by Modulating Tubulin Acetylation via SIRT2 and HDAC6 in Mouse Oocytes

open access: yesFrontiers in Cell and Developmental Biology, 2020
Dynamic changes in microtubules during cell cycle progression are essential for spindle organization to ensure proper segregation of chromosomes. There is growing evidence that post translational modifications of tubulins are the key factors that ...
Hyuk-Joon Jeon, Jeong Su Oh
doaj   +1 more source

Tubulin Acetylation Mediates Bisphenol A Effects on the Microtubule Arrays of Allium cepa and Triticum turgidum

open access: yesBiomolecules, 2019
The effects of bisphenol A (BPA), a prevalent endocrine disruptor, on both interphase and mitotic microtubule array organization was examined by immunofluorescence microscopy in meristematic root cells of Triticum turgidum (durum wheat) and Allium cepa ...
Ioannis-Dimosthenis S. Adamakis   +2 more
doaj   +1 more source

Tau K321/K353 pseudoacetylation within KXGS motifs regulates tau–microtubule interactions and inhibits aggregation

open access: yesScientific Reports, 2021
Alzheimer’s disease is the leading cause of dementia and a defining hallmark is the progressive brain deposition of tau aggregates. The insidious accumulation of brain tau inclusions is also involved in a group of neurodegenerative diseases termed ...
Yuxing Xia   +2 more
doaj   +1 more source

Nutritional stress-induced regulation of microtubule organization and mRNP transport by HDAC1 controlled α-tubulin acetylation

open access: yesCommunications Biology, 2023
In response to nutritional stress, microtubules in cells of the Drosophila female germline are depleted from the cytoplasm and accumulate cortically. This triggers aggregation of mRNPs into large processing bodies (P-bodies) and oogenesis arrest.
Frank Wippich   +3 more
doaj   +1 more source

Acetylated microtubules let the ER slide [PDF]

open access: yesJournal of Cell Biology, 2010
The endoplasmic reticulum (ER) slides along acetylated microtubules, possibly helping it to meet up with other organelles such as mitochondria, [Friedman et al.][1] report. ![Figure][2] The ER (green) slides along a stable microtubule (red).
openaire   +1 more source

Paclitaxel Enhances the Innate Immunity by Promoting NLRP3 Inflammasome Activation in Macrophages

open access: yesFrontiers in Immunology, 2019
Microtubules play critical roles in regulating the activation of NLRP3 inflammasome and microtubule-destabilizing agents such as colchicine have been shown to suppress the activation of this inflammasome.
Qiong-zhen Zeng   +9 more
doaj   +1 more source

dTip60 HAT activity controls synaptic bouton expansion at the Drosophila neuromuscular junction. [PDF]

open access: yesPLoS ONE, 2011
Histone acetylation of chromatin plays a key role in promoting the dynamic transcriptional responses in neurons that influence the neuroplasticity linked to cognitive ability, yet the specific histone acetyltransferases (HATs) that create such epigenetic
Jessica Sarthi, Felice Elefant
doaj   +1 more source

The Effect of Tubulin Acetylation on Microtubule Structure and Dynamics [PDF]

open access: yesBiophysical Journal, 2013
The post-translational acetylation of tubulin is a highly conserved process, but the effect of this modification on microtubule structure and function remains unclear. We have previously reported that the organization and localization of acetylated microtubules changes as epithelial cells undergo apico-basal polarization, suggesting that these ...
Joseph, Elavarasi   +3 more
openaire   +1 more source

Endothelial cell elongation and alignment in response to shear stress requires acetylation of microtubules

open access: yesFrontiers in Physiology
The innermost layer of the vessel wall is constantly subjected to recurring and relenting mechanical forces by virtue of their direct contact with blood flow.
Katiannah Moise   +8 more
doaj   +1 more source

Conserved Lysine Acetylation within the Microtubule-Binding Domain Regulates MAP2/Tau Family Members. [PDF]

open access: yesPLoS ONE, 2016
Lysine acetylation has emerged as a dominant post-translational modification (PTM) regulating tau proteins in Alzheimer's disease (AD) and related tauopathies.
Andrew W Hwang   +6 more
doaj   +1 more source

Home - About - Disclaimer - Privacy