Histone deacetylase 3 indirectly modulates tubulin acetylation

Bacon, Travis J; Seiler, Caroline; Wolny, Marcin; Hughes, Ruth E; Watson, Peter J.; Schwabe, John W. R.; Grigg, R.; Peckham, Michelle

doi:10.1042/bj20150660

Cited by 21 publications

(23 citation statements)

References 49 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…HDAC3 was found in the nucleus and cytoplasm of different cell types (Longworth & Laimins, ; Takami & Nakayama, ). It has been reported that HDAC3 could form a well‐characterized protein complex with the NCoR (nuclear receptor co‐repressors) or homologous SMRT (silencing mediator of retinoic and thyroid receptors) to control the transcriptional activity (Bacon et al, ; Karagianni & Wong, ). Longworth et al also reported that HDAC3 localizes to the plasma membrane and forms a complex with c‐Src to regulate its activity in HFK + 31 cells (Longworth & Laimins, ).…”

Section: Discussionmentioning

confidence: 99%

“…αTAT1 was identified to be the major α‐tubulin acetyltransferase (Kalebic et al, ; Shida, Cueva, Xu, Goodman, & Nachury, ). Recently, Bacon et al found that blocking HDAC3 activity modulates tubulin acetylation in the human prostate cancer line PC3 (Bacon et al, ). Likewise, we previously showed that the acetylation levels of α‐tubulin were dramatically increased in mouse oocytes depleted of HDAC3 (Li et al, ).…”

Section: Discussionmentioning

confidence: 99%

“…For example, in an in vitro reconstituted chromatin system, an HDAC3‐containing protein complex selectively deacetylated histone H3 (Vermeulen et al, ). Blocking HDAC3 activity could dramatically alter the tubulin acetylation in the human prostate cancer cells (Bacon et al, ). In the present study, we identify a substantial reduction of HDAC3 protein in oocytes from old mice.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Loss of HDAC3 contributes to meiotic defects in aged oocytes

Gao

et al. 2019

Aging Cell

View full text Add to dashboard Cite

Maternal age-related decline in oocyte quality is associated with meiotic defects, but the underlying mechanisms remain to be explored. Histone deacetylase 3 (HDAC3) has been shown to govern multiple cellular events via deacetylating diverse substrates. We previously found that HDAC3 could promote meiotic apparatus assembly in mouse oocytes. In the present study, we identified a substantial reduction in HDAC3 protein in oocytes from old mice. Importantly, overexpression of HDAC3 in old oocytes not only partially prevents spindle/chromosome disorganization, but also significantly lowers the incidence of aneuploidy. Meanwhile, we noticed the elevated acetylation level of α-tubulin in oocytes derived from old mice. By employing sitedirected mutagenesis, we showed that acetylation-mimetic mutant tubulin-K40Q disrupts the kinetochore-microtubule attachments and results in the assembly failure of meiotic apparatus in mouse oocytes. Importantly, forced expression of tubulin-K40R (nonacetylatable-mimetic mutant) was capable of alleviating the defective phenotypes of oocytes from aged mice. To sum up, this study uncovers that loss of HDAC3 represents one potential mechanism mediating the effects of advanced maternal age on oocyte quality. K E Y W O R D Saneuploidy, HDACs, maternal aging, oocyte quality, reproduction

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Loss of HDAC3 contributes to meiotic defects in aged oocytes

Gao

et al. 2019

Aging Cell

View full text Add to dashboard Cite

show abstract

“…Indeed, by controlling the p300 activity, SIRT2 could have an impact on the activity as well as the localization of HDAC6. HDAC3 has also been reported to indirectly control the state of α-tubulin K40 acetylation [84]. HDAC3 has also been reported to indirectly control the state of α-tubulin K40 acetylation [84].…”

Section: Regulation Of α-Tubulin K40 Acetylationmentioning

confidence: 99%

The growing landscape of tubulin acetylation: lysine 40 and many more

Sadoul

Khochbin

2016

Biochemical Journal

View full text Add to dashboard Cite

Tubulin heterodimers are the building block of microtubules, which are major elements of the cytoskeleton. Several types of post-translational modifications are found on tubulin subunits as well as on the microtubule polymer to regulate the multiple roles of microtubules. Acetylation of lysine 40 (K40) of the α-tubulin subunit is one of these post-translational modifications which has been extensively studied. We summarize the current knowledge about the structural aspects of K40 acetylation, the functional consequences, the enzymes involved and their regulation. Most importantly, we discuss the potential importance of the recently discovered additional acetylation acceptor lysines in tubulin subunits and highlight the urgent need to study tubulin acetylation in a more integrated perspective.

show abstract

“…This post translational modification is a hallmark of stability because it increases mechanical resilience to ensure the persistence of long-lived microtubules (Xu et al, 2017b) (Janke and Montagnac, 2017). Its downregulation, resulting from either HDACs inhibition or GSK3β activation, has been correlated to microtubule dynamics alteration in different cell types (Garza et al, 2018) (Bacon et al, 2015) (Qu et al, 2017). In these cells, Dock5 acts as a key signaling adaptor that brings Akt into the vicinity of GSK3β, allowing it to phosphorylate GSK3β on serine 9 and inhibit its activity (Ogawa et al, 2014).…”

Section: Discussionmentioning

confidence: 99%

Dock5 is a new regulator of microtubule dynamic instability through GSK3β inhibition in osteoclasts

Guimbal

Guérit

et al. 2019

Preprint

View full text Add to dashboard Cite

Background information:Osteoclast resorption is dependent on a podosome-rich structure, called sealing zone, which is stabilized by acetylated microtubules. It tightly attaches the osteoclast to the bone creating a favorable acidic microenvironment for bone degradation. We already established that Rac activation by Dock5 is necessary for osteoclast resorption. Indeed, inhibition of Dock5 in osteoclasts results in Rac1 decreased activity associated to impaired podosome assembly into sealing zones and resorbing activity. Results:In this report, we show that Dock5 knockout osteoclasts also present a reduced acetylated tubulin level leading to a decreased length and duration of microtubule growth phases whereas their growth speed remains unaffected. Dock5 does not act by direct interaction with the polymerized tubulin but through inhibition of the microtubules destabilizing kinase GSK3β downstream of Akt activation.Interestingly, we ruled out the implication of Rac1 in this process using specific inhibitors. Conclusion:Our data involve Dock5 as a new regulator of microtubule dynamic instability in osteoclast. Significance:The fact that Dock5 is a regulator of both actin cytoskeleton and microtubule dynamics makes it an interesting therapeutic target for osteolytic pathologies because of its dual role on sealing zone formation and stabilization.

show abstract

Histone deacetylase 3 indirectly modulates tubulin acetylation

Cited by 21 publications

References 49 publications

Loss of HDAC3 contributes to meiotic defects in aged oocytes

Loss of HDAC3 contributes to meiotic defects in aged oocytes

The growing landscape of tubulin acetylation: lysine 40 and many more

Dock5 is a new regulator of microtubule dynamic instability through GSK3β inhibition in osteoclasts

Contact Info

Product

Resources

About