Results 11 to 20 of about 292,166 (345)
The Tubulin Code and Tubulin-Modifying Enzymes in Autophagy and Cancer [PDF]
Cancers, 2021 Microtubules are key components of the cytoskeleton of eukaryotic cells. Microtubule dynamic instability together with the “tubulin code” generated by the choice of different α- and β- tubulin isoforms and tubulin post-translational modifications have essential roles in the control of a variety of cellular processes, such as cell shape, cell motility ...
Trisciuoglio Daniela, Degrassi Francesca
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The tubulin code at a glance [PDF]
Journal of Cell Science, 2017 ABSTRACT Microtubules are key cytoskeletal elements of all eukaryotic cells and are assembled of evolutionarily conserved α-tubulin–β-tubulin heterodimers. Despite their uniform structure, microtubules fulfill a large diversity of functions.
Sudarshan Gadadhar +3 more
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Autopalmitoylation of tubulin [PDF]
Protein Science, 2000 AbstractPure rat brain tubulin is readily palmitoylated in vitro using [3H]palmitoyl CoA but no added enzymes. A maximum of approximately six palmitic acids are added per dimer in 2–3 h at 36–37 °C under native conditions. Both α and β tubulin are labeled, and 63–73% of the label was hydroxylamine‐labile, presumed thioesters.
P. J. Britto +3 more
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Cell Cycle, 2007 Microtubules create diverse arrays with specific cellular functions such as the mitotic spindle, cilia and bundles inside neurons. How microtubules are regulated to enable specific functions is not well understood. Recent work has shown that posttranslational modifications of the tubulin building blocks mark subpopulations of microtubules and ...
Kristen J. Verhey, Jacek Gaertig
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Frontiers in Cell and Developmental Biology, 2023 Microtubules are filamentous structures that play a critical role in a diverse array of cellular functions including, mitosis, nuclear translocation, trafficking of organelles and cell shape. They are composed of α/β-tubulin heterodimers which are encoded by a large multigene family that has been implicated in an umbrella of disease states collectively
Thomas D. Cushion +5 more
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γ-Tubulin 2 nucleates microtubules and is downregulated in mouse early embryogenesis.
PLoS ONE, 2012 γ-Tubulin is the key protein for microtubule nucleation. Duplication of the γ-tubulin gene occurred several times during evolution, and in mammals γ-tubulin genes encode proteins which share ∼97% sequence identity.
Stanislav Vinopal +7 more
doaj +1 more source
eLife, 2015 Microtubule dynamics and polarity stem from the polymerization of αβ-tubulin heterodimers. Five conserved tubulin cofactors/chaperones and the Arl2 GTPase regulate α- and β-tubulin assembly into heterodimers and maintain the soluble tubulin pool in the ...
Stanley Nithianantham +7 more
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Effects of α-tubulin acetylation on microtubule structure and stability
Proceedings of the National Academy of Sciences of the United States of America, 2019 Significance Microtubules are polymers of αβ-tubulin that play important roles in the cell. Regulation of their dynamics is critical for function and includes the posttranslational modification of tubulin.
L. Eshun-Wilson +9 more
semanticscholar +1 more source
Proteolysis of tubulin and the substructure of the tubulin dimer.
Journal of Biological Chemistry, 1986 The alpha and beta subunits of tubulin each have a single highly reactive site for a variety of proteases that divides each subunit into two unequal regions. The position of cleavage is not the same for alpha and beta, since alpha is consistently cleaved into about 38- and 14-kDa pieces, while beta is cleaved into about 34- and 21-kDa pieces.
D L Sackett, J Wolff
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Tubulin acetylation protects long-lived microtubules against mechanical aging
Nature Cell Biology, 2017 Long-lived microtubules endow the eukaryotic cell with long-range transport abilities. While long-lived microtubules are acetylated on Lys40 of α-tubulin (αK40), acetylation takes place after stabilization and does not protect against depolymerization ...
D. Portran +4 more
semanticscholar +1 more source