Browse our anti-TUBA1A (Tuba1a) Antibodies

Human Tubulin, alpha 1a (Tuba1a) interaction partners

1. These data unequivocally show that free tubulin dimers represent the preferred HDAC6 substrate, with a K M value of 0.23 microM and a deacetylation rate over 1,500-fold higher than that of assembled microtubules.

2. Low Tubulin expression is associated with liver cancer.

3. A de novo heterozygous c.320A>G [p.(His 107 Arg)] mutation in TUBA1A was identified in a patient with microcephaly, epileptic seizures, and severe developmental delay.

4. Given that Spastin engages the MT in two places, we propose that severing occurs by forces exerted on the C-terminal tail of tubulin, which results in a conformational change in tubulin, which releases it from the polymer.

5. Molecular docking studies revealed that 6f interacted and bound ef fi ciently with the colchicine-binding site of tubulin. In addition, 6f treatment induced G2/M cell cycle arrest dose-dependently and subsequently induced cell apoptosis

6. induced pluripotent stem cells (iPSCs) from the umbilical cord and peripheral blood of two lissencephaly patients with different clinical severities carrying alpha tubulin (TUBA1A) missense mutations, were generated.

7. Long intergenic non-coding RNA APOC1P1-3 inhibits apoptosis by decreasing alpha-tubulin acetylation in breast cancer.

8. 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.

9. 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

10. Data show that tubulin phosphorylation and acetylation play important roles in the control of microtubule assembly and stability.

11. Data show that plasma membrane Ca(2+)-ATPase (PMCA) was associated with tubulin in normotensive and hypertensive erythrocytes.

12. Data suggest that tubulin functionally interact with the vimentin network in a cell-type specific manner.

13. Studies indicate that alpha-tubulin acetylation and microtubule level is mainly governed by opposing actions of alpha-tubulin acetyltransferase 1 (ATAT1) and histone deacetylase 6 (HDAC6).

14. Data from studies using peptide fragment of alpha-tubulin (residues 31-49) suggest that Ser38 is crucial for substrate recognition by alpha-tubulin acetylase 1 (ATAT1); Asp39, Ile42, the glycine stretch (residues 43-45), and Asp46 are also involved.

15. Lysine 40 acetylation of alpha-tubulin does not result in significant changes in kinesin-1's landing rate or motility parameters.

16. These results demonstrated that SelP interacts with tubulin, alpha 1a (TUBA1A).

17. This study show all foetuses with lissencephaly and cerebellar hypoplasia carried distinct TUBA1A mutations.

18. These findings call attention to PKC-mediated phosphorylation of alpha-tubulin as a novel mechanism for controlling the dynamics of microtubules that result in cell movement.

19. case provides new insight into the wide spectrum of disease phenotypes associated with TUBA1A mutation

20. The present study confirms that mutations in tubulin genes are responsible for complex brain malformation.

Mouse (Murine) Tubulin, alpha 1a (Tuba1a) interaction partners

1. In this study, we demonstrate that missense mutations affecting arginine at position 402 (R402) of TUBA1A alpha-tubulin selectively impair dynein motor activity and severely and dominantly disrupt cortical neuronal migration.

2. Transgenic mdx mice expressing the short dystrophin isoform Dp116 served as a negative control. All mini- and micro-dystrophins restored elevated detyrosinated alpha-tubulin and microtubule density of mdx muscle to values not different from C57BL/10, however, only mini-dystrophins restored the transverse component of the microtubule lattice back to C57BL/10.

3. Here the authors demonstrate that mice lacking the alpha-tubulin acetyltransferase Atat1 in sensory neurons display profound deficits in their ability to detect mechanical stimuli.

4. 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.

5. Further PS treatment resulted in recovery of axonal outgrowth and enhanced retrograde axonal transport by decreasing histone deacetylase 6 (HDAC6) levels and thus increasing acetylation of alpha-tubulin 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

6. mass spectrometry-based quantitative comparison of acetylated peptides from wild-type vs HDAC6 knockout mice allowed to identify six new deacetylation sites possibly mediated by HDAC6.

7. These results give new insights into the functions of Tuba1a, mechanisms for regulating tubulin proteostasis, and how compromising these may lead to neural defects.

8. Data indicate that alpha 1a tubulin (Tuba1a) showed the least variability in expression among the different stages of lung development.

9. Tubulin-tyrosine ligase (TTL) is required to increase the levels of tyrosinated alpha-tubulin at the axon injury site and plays an important role in injury signaling.

10. Data suggest a mechanistic link between tubulin hyperacetylation and autophagy induction.

11. TFIIB co-localizes and interacts with alpha-tubulin during oocyte meiosis in the mouse and depletion of TFIIB causes arrest of subsequent embryo development.

12. Acetylation of alpha-tubulin is under the control of the acetyltransferase MEC-17 and deacetylases SIRT2 (Sirtuin 2) and HDAC6 (histone deacetylase 6). Adipocyte development is inhibited in MEC-17-knockdown cells, but enhanced in MEC-17-overexpressing cells.

13. Unambiguous identification of novel glutamylation sites E441 and E443 in mouse brain Tuba1a and Tuba1b.

14. This study demonistrated that novel tubal(aspartic acid to glycine) mutant mouse is a novel animal model for neurodevelopmental disorders.

15. These results demonstrate a role for CCP1 in the processing of Glu residues from beta- as well as alpha-tubulin in vitro and in vivo.

16. Our results highlight the importance of Tuba1a for correct neuronal migration

17. association between dysferlin and alpha-tubulin, as well as between dysferlin and microtubules

18. mice harbouring an S140G mutation in Tuba1a present with normal neurogenic potential, but that this neurogenesis is often ectopic

19. Data indicated that CacyBP/SIP could simultaneously interact with tubulin and actin, suggesting that CacyBP/SIP might link actin and tubulin cytoskeletons.

20. Data support a model in which stathmin functions in interphase to control the partitioning of tubulins between dimer and polymer pools by setting the number of microtubules per cell.

Cow (Bovine) Tubulin, alpha 1a (Tuba1a) interaction partners

1. Lys40 of alpha-tubulin acetylation directly weakens inter-protofilament interactions.

2. the role of the human TBCE and TBCB chaperones in alpha-tubulin-beta-tubulin dissociation, was investigated.

3. Lysine 40 acetylation of alpha-tubulin does not result in significant changes in kinesin-1's landing rate or motility parameters.

4. Data suggest presence of unstructured C-terminal tubulin tail in Vdac1 pore (voltage-dependent anion channel 1) decreases pore's conductance and switches pore's selectivity from anionic to cationic rendering ATP transport virtually impossible.

5. TTL has specifically evolved to recognize and modify tubulin.

6. VDAC phosphorylation is an important determinant of its interaction with dimeric tubulin.