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induced pluripotent stem cells (iPSCs) from the umbilical cord and peripheral blood of two lissencephaly patients with different clinical severities carrying alpha tubulin (show TUBA4A Proteins) (TUBA1A) missense mutations, were generated.
Long intergenic non-coding RNA APOC1P1-3 inhibits apoptosis by decreasing alpha-tubulin (show TUBA4A Proteins) acetylation in breast cancer.
Results show that Tuba1a plays an essential, noncompensated role in neuronal saltatory migration in vivo and highlight the importance of microtubule flexibility in nucleus-centrosome coupling and neuronal-branching regulation during neuronal migration.
data suggest that the TUBA1A mutations disrupting lateral interactions have pronounced dominant-negative effects on microtubule dynamics that are associated with the severe end of the lissencephaly spectrum
Data show that tubulin (show TUBB Proteins) phosphorylation and acetylation play important roles in the control of microtubule assembly and stability.
Data show that plasma membrane Ca(2+)-ATPase (show ATP2B2 Proteins) (PMCA) was associated with tubulin (show TUBB Proteins) in normotensive and hypertensive erythrocytes.
Data suggest that tubulin (show TUBB Proteins) functionally interact with the vimentin (show VIM Proteins) network in a cell-type specific manner.
Studies indicate that alpha-tubulin (show TUBA4A Proteins) acetylation and microtubule level is mainly governed by opposing actions of alpha-tubulin acetyltransferase 1 (ATAT1 (show C6orf134 Proteins)) and histone deacetylase 6 (HDAC6 (show HDAC6 Proteins)).
Data from studies using peptide fragment of alpha-tubulin (show TUBA4A Proteins) (residues 31-49) suggest that Ser38 is crucial for substrate recognition by alpha-tubulin (show TUBA4A Proteins) acetylase 1 (ATAT1 (show C6orf134 Proteins)); Asp39, Ile42, the glycine stretch (residues 43-45), and Asp46 are also involved.
Lysine 40 acetylation of alpha-tubulin (show TUBA4A Proteins) does not result in significant changes in kinesin-1's landing rate or motility parameters.
Here the authors demonstrate that mice lacking the alpha-tubulin (show TUBA4A Proteins) acetyltransferase Atat1 (show C6orf134 Proteins) in sensory neurons display profound deficits in their ability to detect mechanical stimuli.
Collectively, these findings suggest that Smo and primary cilia-dependent noncanonical Hh signaling leads to post-translational regulation of microtubules and may be important for modulating cell behaviors.
Further PS treatment resulted in recovery of axonal outgrowth and enhanced retrograde axonal transport by decreasing histone deacetylase 6 (HDAC6 (show HDAC6 Proteins)) levels and thus increasing acetylation of alpha-tubulin (show TUBA4A Proteins) levels. Thus, we have identified the molecular pathway that leads to neurodegeneration in FD and have demonstrated that phosphatidylserine treatment has the potential to slow progression of neurodegeneration
mass spectrometry-based quantitative comparison of acetylated peptides from wild-type vs HDAC6 (show HDAC6 Proteins) knockout mice allowed to identify six new deacetylation sites possibly mediated by HDAC6 (show HDAC6 Proteins).
These results give new insights into the functions of Tuba1a, mechanisms for regulating tubulin (show TUBB Proteins) proteostasis, and how compromising these may lead to neural defects.
Data indicate that alpha 1a tubulin (show TUBB Proteins) (Tuba1a) showed the least variability in expression among the different stages of lung development.
Tubulin-tyrosine ligase (TTL (show TTL Proteins)) is required to increase the levels of tyrosinated alpha-tubulin (show TUBA4A Proteins) at the axon injury site and plays an important role in injury signaling.
Data suggest a mechanistic link between tubulin (show TUBB Proteins) hyperacetylation and autophagy induction.
TFIIB (show GTF2B Proteins) co-localizes and interacts with alpha-tubulin (show TUBA4A Proteins) during oocyte meiosis in the mouse and depletion of TFIIB (show GTF2B Proteins) causes arrest of subsequent embryo development.
Acetylation of alpha-tubulin (show TUBA4A Proteins) is under the control of the acetyltransferase MEC-17 (show C6orf134 Proteins) and deacetylases SIRT2 (Sirtuin 2 (show SIRT2 Proteins)) and HDAC6 (histone deacetylase 6 (show HDAC6 Proteins)). Adipocyte development is inhibited in MEC-17 (show C6orf134 Proteins)-knockdown cells, but enhanced in MEC-17 (show C6orf134 Proteins)-overexpressing cells.
Lys40 of alpha-tubulin (show TUBA4A Proteins) acetylation directly weakens inter-protofilament interactions.
the role of the human TBCE and TBCB (show TBCB Proteins) chaperones in alpha-tubulin (show TUBA4A Proteins)-beta-tubulin (show TUBB Proteins) dissociation, was investigated.
Data suggest presence of unstructured C-terminal tubulin (show TUBB Proteins) tail in Vdac1 (show VDAC1 Proteins) pore (voltage-dependent anion channel 1 (show VDAC1 Proteins)) decreases pore's conductance and switches pore's selectivity from anionic to cationic rendering ATP transport virtually impossible.
TTL (show TTL Proteins) has specifically evolved to recognize and modify tubulin (show TUBB Proteins).
VDAC phosphorylation is an important determinant of its interaction with dimeric tubulin (show TUBB Proteins).
LRRK2 (show LRRK2 Proteins) plays an important role as a physiological regulator for phosphorylation-mediated dissociation of tau from microtubules.
Microtubules of the eukaryotic cytoskeleton perform essential and diverse functions and are composed of a heterodimer of alpha and beta tubulins. The genes encoding these microtubule constituents belong to the tubulin superfamily, which is composed of six distinct families. Genes from the alpha, beta and gamma tubulin families are found in all eukaryotes. The alpha and beta tubulins represent the major components of microtubules, while gamma tubulin plays a critical role in the nucleation of microtubule assembly. There are multiple alpha and beta tubulin genes, which are highly conserved among species. This gene encodes alpha tubulin and is highly similar to the mouse and rat Tuba1 genes. Northern blotting studies have shown that the gene expression is predominantly found in morphologically differentiated neurologic cells. This gene is one of three alpha-tubulin genes in a cluster on chromosome 12q. Mutations in this gene cause lissencephaly type 3 (LIS3) - a neurological condition characterized by microcephaly, mental retardation, and early-onset epilepsy and caused by defective neuronal migration. Alternative splicing results in multiple transcript variants encoding distinct isoforms.
, tubulin alpha-1 chain
, tubulin alpha-1A chain
, tubulin, alpha 1
, tubulin B-alpha-1
, tubulin alpha-3 chain
, tubulin, alpha, brain-specific
, alpha-tubulin 3
, tubulin, alpha 3
, Talpha1 alpha-tubulin
, alpha-tubulin isotype M-alpha-1
, alpha-tubulin ubiquitous
, tubulin K-alpha-1
, tubulin alpha-1B chain
, tubulin alpha-ubiquitous chain
, tubulin, alpha 1a
, tubulin alpha-1A chain-like
, Alpha-tubulin 1
, Tubulin alpha-1 chain
, tubulin alpha 3
, Alpha-tubulin 2
, Alpha-tubulin II
, Tubulin alpha-2 chain
, alpha-tubulin II
, tubulin alpha 1a L homeolog