@article {47371,
	title = {Extracellular HDAC6 ZnF UBP domain modulates the actin network and post-translational modifications of Tau},
	journal = {Cell Communication and Signaling},
	volume = {19},
	year = {2021},
	month = {MAY },
	pages = {49},
	type = {Article},
	abstract = {<p>Background: Microtubule-associated protein Tau undergoes aggregation in Alzheimer{\textquoteleft}s disease (AD) and a group of other related diseases collectively known as Tauopathies. In AD, Tau forms aggregates, which are deposited intracellularly as neurofibrillary tangles. Histone deacetylase-6 (HDAC6) plays an important role in aggresome formation, where it recruits polyubiquitinated aggregates to the motor protein dynein. Methods: Here, we have studied the effects of HDAC6 ZnF UBP on Tau phosphorylation, ApoE localization, GSK-3 beta regulation and cytoskeletal organization in neuronal cells by immunocytochemical analysis. This analysis reveals that the cell exposure to the UBP-type zinc finger domain of HDAC6 (HDAC6 ZnF UBP) can modulate Tau phosphorylation and actin cytoskeleton organization. Results: HDAC6 ZnF UBP treatment to cells did not affect their viability and resulted in enhanced neurite extension and formation of structures similar to podosomes, lamellipodia and podonuts suggesting the role of this domain in actin re-organization. Also, HDAC6 ZnF UBP treatment caused increase in nuclear localization of ApoE and tubulin localization in microtubule organizing centre (MTOC). Therefore, our studies suggest the regulatory role of this domain in different aspects of neurodegenerative diseases. Upon HDAC6 ZnF UBP treatment, inactive phosphorylated form of GSK-3 beta increases without any change in total GSK-3 beta level. Conclusions: HDAC6 ZnF UBP was found to be involved in cytoskeletal re-organization by modulating actin dynamics and tubulin localization. Overall, our study suggests that ZnF domain of HDAC6 performs various regulatory functions apart from its classical function in aggresome formation in protein misfolding diseases.</p>},
	keywords = {Actin, Cytoskeleton, HDAC6, Microtubule, neurodegeneration, Phosphorylation, Podonut, Podosomes, Tau, Tauopathies},
	doi = {10.1186/s12964-021-00736-9},
	author = {Balmik, Abhishek Ankur and Sonawane, Shweta Kishor and Chinnathambi, Subashchandrabose}
}
@article {48109,
	title = {Histone deacetylase-6 modulates Tau function in Alzheimer{\textquoteright}s disease},
	journal = {Biochimica Et Biophysica Acta-Molecular Cell Research},
	volume = {1869},
	year = {2022},
	month = {AUG},
	pages = {119275},
	type = {Article},
	abstract = {<p>
	Alzheimer{\textquoteright}s disease (AD), one of the major tauopathies, is multifactorial with a massive demand for disease modifying treatments rather than symptom management. An AD-affected neuron shows Tau depositions generated due to overload on the proteostasis machinery of the cell and/or abnormal post-translational modifications on Tau protein. Loss of memory or dementia is the most significant concern in AD, occurring due to the loss of neurons and the connections between them. In a healthy brain, neurons interact with the environment and each other through extensions and migratory structures. It can thus be safe to assume that Tau depositions affect these growth structures in neurons. A Histone Deacetylase, HDAC6, has shown elevated levels in AD while also demonstrating direct interaction with the Tau protein. HDAC6 interacts with multiple proteins in the cell and is possibly involved in various signalling pathways. Its deacetylase activity has been a point of controversy in AD; however other functional domains remain unexplored. This review highlights the beneficial potential of HDAC6 in AD in mediating both Tau proteostasis and cytoskeletal rewiring for the neuritic extensions through its Ubiquitin Binding domain (HDAC6 ZnF UBP).</p>
},
	keywords = {Actin, Cytoskeleton, HDAC6, Microtubules, Proteostasis, Tau, ZnF UBP domain},
	issn = {0167-4889},
	doi = {10.1016/j.bbamcr.2022.119275},
	author = {Qureshi, Tazeen and Chinnathambi, Subashchandrabose}
}
@article {47808,
	title = {Inter-relationship of Histone Deacetylase-6 with Tau-cytoskeletal organization and remodeling},
	journal = {European Journal of Cell Biology},
	volume = {101},
	year = {2022},
	month = {APR},
	pages = {151202},
	type = {Article},
	abstract = {Cytoskeletal elements are the key players in cellular integrity, structure, signalling and migration. Each cytoskeletal element comprises of properties with respect to its structure and stability, which serve a specific array of functions. These structures are highly dynamic and regulated by modulation via direct interaction or post-translational modifications. HDAC6 is a cytoplasmic deacetylase known to regulate a wide range of cellular functions either through its deacetylase activity or direct interaction via its C-terminal ZnF UBP domain. HDAC6 has been widely studied for its role in aggresome formation, which acts as a protective mechanism upon protein aggregation. HDAC6 is known to play a critical role in the regulation of cytoskeletal elements-microtubules and actin filaments. This review summarizes the regulatory role of HDAC6 in cytoskeletal remodeling and dynamics of neuronal cells and its significance in neurodegenerative diseases.},
	keywords = {Actin, Cell migration, Cytoskeleton remodeling, HDAC6, Microtubules, Podosomes, ZnF UBP},
	issn = {0171-9335},
	doi = {10.1016/j.ejcb.2022.151202},
	author = {Abhishek Ankur Balmik and Subashchandrabose Chinnathambi}
}
