Deacetylation of α-tubulin and cortactin is required for HDAC6 to trigger ciliary disassembly

Ran, Jie; Yang, Yunfan; Li, Dengwen; Liu, Min; Zhou, Jun

doi:10.1038/srep12917

Cited by 135 publications

(142 citation statements)

References 46 publications

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“…Additional studies will be needed to identify the mechanisms through which HEF1 (NEDD9) is upregulated and recruited to basal bodies following mitogen stimulation. Recent studies have uncovered another critical effector of HDAC6 activity, cortactin, which promotes actin polymerization 54 . Given that acetylation of cortactin abrogates its interaction with filamentous actin and that actin polymerization counteracts cilium assembly, de-acetylation of cortactin could further explain how HDAC6 activation promotes cilium disassembly by enhancing actin polymerization.…”

Section: Cilium Disassemblymentioning

confidence: 99%

Cilium assembly and disassembly

2016

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The primary cilium is an antenna-like, immotile organelle present on most types of mammalian cells, which interprets extracellular signals that regulate growth and development. Although once considered a vestigial organelle, the primary cilium is now the focus of considerable interest. We now know that ciliary defects lead to a panoply of human diseases, termed ciliopathies, and the loss of this organelle may be an early signature event during oncogenic transformation. Ciliopathies include numerous seemingly unrelated developmental syndromes, with involvement of the retina, kidney, liver, pancreas, skeletal system and brain. Recent studies have begun to clarify the key mechanisms that link cilium assembly and disassembly to the cell cycle, and suggest new possibilities for therapeutic intervention.

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Section: Cilium Disassemblymentioning

confidence: 99%

Cilium assembly and disassembly

2016

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“…Interestingly, HDAC6‐mediated deacetylation of α‐tubulin and cortactin was recently reported to play a role in ciliary disassembly . DISC1 and other centrosomal proteins are also located at the base of primary cilia, and these collective findings suggest similar mechanisms of acetylation are required for both processes.…”

Section: Camdi Represses Hdac6 Activity To Promote Centrosome Stabilimentioning

confidence: 96%

Neurons acetylate their way to migration

Borrie

Bagni

2016

EMBO Reports

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The centrosome is crucial for neuronal migration and polarisation, processes that are disrupted in a number of neurodevelopmental disorders including schizophrenia. Mutation of DISC1, associated with increased risk of schizophrenia and psychiatric illness, has been shown to affect the centrosome, but the mechanisms involved have not been elucidated. In this issue of EMBO Reports, Fukuda and colleagues demonstrate that a DISC1‐interacting protein, CAMDI, suppresses the activity of the histone deacetylase HDAC6, thereby promoting centrosome stability and consequently neuronal migration . Loss of CAMDI leads to cortical migration defects and behavioural phenotypes that model autism spectrum disorders and which can be rescued by inhibition of HDAC6. The study provides novel mechanistic insight into centrosome regulation in neurodevelopment.

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“…In this Commentary, we have discussed the involvement of CYLD in cell migration, cell cycle progression, chemotherapeutic drug sensitivity and ciliogenesis through various mechanisms that are largely dependent on its regulation of microtubules. In addition, CYLD might also participate in other microtubule-dependent activities, such as intracellular transport, because CYLD inhibits the deacetylase activity of HDAC6 and HDAC6-mediated α-tubulin deacetylation is likely to affect intracellular transport along microtubules (Dompierre et al, 2007;Kaul et al, 2014;Reed et al, 2006;Walter et al, 2012). CYLD also regulates the activation of small Rho GTPases, such as RhoA and Rac1, suggesting that it might play a role in coordinating the actions of microtubules and actin filaments Yang et al, 2013).…”

Section: Discussionmentioning

confidence: 99%

CYLD – a deubiquitylase that acts to fine-tune microtubule properties and functions

Yang

Zhou

2016

Journal of Cell Science

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Microtubules are dynamic structures that are crucially involved in a variety of cellular activities. The dynamic properties and functions of microtubules are regulated by various factors, such as tubulin isotype composition and microtubule-binding proteins. Initially identified as a deubiquitylase with tumor-suppressing functions, the protein cylindromatosis (CYLD) has recently been revealed to interact with microtubules, modulate microtubule dynamics, and participate in the regulation of cell migration, cell cycle progression, chemotherapeutic drug sensitivity and ciliogenesis. These findings have greatly enriched our understanding of the roles of CYLD in physiological and pathological conditions. Here, we focus on recent literature that shows how CYLD impacts on microtubule properties and functions in various biological processes, and discuss the challenges we face when interpreting results obtained from different experimental systems.

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Deacetylation of α-tubulin and cortactin is required for HDAC6 to trigger ciliary disassembly

Cited by 135 publications

References 46 publications

Cilium assembly and disassembly

Cilium assembly and disassembly

Neurons acetylate their way to migration

CYLD – a deubiquitylase that acts to fine-tune microtubule properties and functions

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