Human histone deacetylase 6 shows strong preference for tubulin dimers over assembled microtubules

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F17%3A00480758" target="_blank" >RIV/86652036:_____/17:00480758 - isvavai.cz</a>
Alternative codes found
RIV/61388963:_____/17:00480758 RIV/00216208:11310/17:10362555
Result on the web
<a href="http://dx.doi.org/10.1038/s41598-017-11739-3" target="_blank" >http://dx.doi.org/10.1038/s41598-017-11739-3</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s41598-017-11739-3" target="_blank" >10.1038/s41598-017-11739-3</a>

Result language
angličtina
Original language name
Human histone deacetylase 6 shows strong preference for tubulin dimers over assembled microtubules
Original language description
Human histone deacetylase 6 (HDAC6) is the major deacetylase responsible for removing the acetyl group from Lys40 of alpha-tubulin (alpha K40), which is located lumenally in polymerized microtubules. Here, we provide a detailed kinetic analysis of tubulin deacetylation and HDAC6/microtubule interactions using individual purified components. Our data unequivocally show that free tubulin dimers represent the preferred HDAC6 substrate, with a K-M value of 0.23 mu M and a deacetylation rate over 1,500-fold higher than that of assembled microtubules. We attribute the lower deacetylation rate of microtubules to both longitudinal and lateral lattice interactions within tubulin polymers. Using TIRF microscopy, we directly visualized stochastic binding of HDAC6 to assembled microtubules without any detectable preferential binding to microtubule tips. Likewise, indirect immunofluorescence microscopy revealed that microtubule deacetylation by HDAC6 is carried out stochastically along the whole microtubule length, rather than from the open extremities. Our data thus complement prior studies on tubulin acetylation and further strengthen the rationale for the correlation between tubulin acetylation and microtubule age.
Czech name
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Czech description
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Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology

Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2017
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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