Centaurin-α₂ interacts with β-tubulin and stabilizes microtubules. [PDF]
Centaurin-α₂ is a GTPase-activating protein for ARF (ARFGAP) showing a diffuse cytoplasmic localization capable to translocate to membrane, where it binds phosphatidylinositols. Taking into account that Centaurin-α₂ can localize in cytoplasm and that its
Paola Zuccotti +8 more
doaj +3 more sources
Linking acetylated α-Tubulin redistribution to α-Synuclein pathology in brain of Parkinson’s disease patients [PDF]
Highly specialized microtubules in neurons are crucial to both health and disease of the nervous system, and their properties are strictly regulated by different post-translational modifications, including α-Tubulin acetylation.
Samanta Mazzetti +12 more
doaj +2 more sources
Matrix stiffness‐induced α‐tubulin acetylation is required for skin fibrosis formation through activation of Yes‐associated protein [PDF]
Skin fibrosis, a pathological process featured by fibroblast activation and extracellular matrix (ECM) deposition, makes a significant contribution to morbidity.
Dongsheng Wen +8 more
doaj +2 more sources
Ethanol Administration in Mice Leads to Sex-Specific Changes in the Acetylation of α-Tubulin in the Cerebellum [PDF]
Background: Acetylation of α-tubulin is an important post-translational modification that helps maintain microtubules’ stability and dynamics, including axonal transport, cell signaling, and overall neuronal integrity.
Abosede Elesinnla +5 more
doaj +2 more sources
MFN2 coordinates mitochondria motility with α-tubulin acetylation and this regulation is disrupted in CMT2A [PDF]
Summary: Mitofusin-2 (MFN2), a large GTPase residing in the mitochondrial outer membrane and mutated in Charcot-Marie-Tooth type 2 disease (CMT2A), is a regulator of mitochondrial fusion and tethering with the ER.
Atul Kumar +10 more
doaj +2 more sources
Acetylated α-Tubulin and α-Synuclein: Physiological Interplay and Contribution to α-Synuclein Oligomerization. [PDF]
Emerging evidence supports that altered α-tubulin acetylation occurs in Parkinson's disease (PD), a neurodegenerative disorder characterized by the deposition of α-synuclein fibrillary aggregates within Lewy bodies and nigrostriatal neuron degeneration ...
Calogero AM +8 more
europepmc +4 more sources
Modulating microtubule stability via α-tubulin acetylation partially restores Golgi fragmentation in spinal muscular atrophy. [PDF]
Background/aim: Spinal muscular atrophy (SMA) is a neurodegenerative disease caused by the loss of survival of motor neuron (SMN) protein. SMN deficiency leads to perturbations of the cytoskeleton, including microtubules, which are mainly involved in ...
Zobaroğlu Özer P +9 more
europepmc +2 more sources
Corrigendum to: âGenetic polymorphism at the β-tubulin locus among human and animal isolates ofCryptosporidium parvumâ [PDF]
The authors would like to make the following correction: In Fig. 1 on page 176, a base (an Adenine) is …
Simone Cacciò +3 more
openaire +1 more source
Background Reversible acetylation of α-tubulin has been implicated in modulating microtuble structures and functions, which may subsequently involve in cellular apoptosis and autophage.
Qilin Wang, Xiangguo Liu
doaj +1 more source
Sequence diversity of β-tubulin (tubA) gene inPhaeosphaeria nodorumandP. avenaria [PDF]
Full-length coding sequences of the beta-tubulin gene (tubA) were PCR-amplified and sequenced from 42 Phaeosphaeria isolates, including 16 P. nodorum and 23 P. avenaria species from cereals, two Polish isolates from rye (Secale cereale L.), and one isolate from dallis grass (Paspalum dilatatum Poir).
Arkadiusz, Malkus +5 more
openaire +2 more sources

