Implications of valosin-containing protein in promoting autophagy to prevent tau aggregation
Title | Implications of valosin-containing protein in promoting autophagy to prevent tau aggregation |
Publication Type | Journal Article |
Year of Publication | 2021 |
Authors | Chinnathambi, S, Gorantla, NVijay |
Journal | Neuroscience |
Volume | 476 |
Pagination | 125-134 |
Date Published | NOV |
Type of Article | Review |
ISSN | 0306-4522 |
Keywords | Autophagy, segregase, Tau aggregates, Ubiquitin-proteasome system, valosin-containing protein |
Abstract | and cellular degradative mechanisms modulate Tau aggregation. During aging and neu-rodegenerative disorders, the cellular proteostasis is disturbed due to impaired protective mechanisms. This results in accumulation of aberrant Tau aggregates in the neuron that leads to microtubule destabilization and neuronal degeneration. The intricate mechanisms to prevent Tau aggregation involve chaperones, autophagy, and proteasomal system have gained main focus about concerning to therapeutic intervention. However, the thor-ough understanding of other key proteins, such as Valosin-containing protein (VCP), is limited. In various neu-rodegenerative diseases, the chaperone-like activity of VCP is involved in preventing protein aggregation and mediating the degradation of aberrant proteins by proteasome and autophagy. In the case of Tau aggregation associated with Alzheimer's disease, the importance of VCP is poorly understood. VCP is known to co-localize with Tau, and alterations in VCP cause aberrant accumulation of Tau. Nevertheless, the direct mechanism of VCP in altering Tau aggregation is not known. Hence, we speculate that VCP might be one of the key modulators in preventing Tau aggregation and can disintegrate Tau aggregates by directing its clearance by autophagy. = 2021 IBRO. Published by Elsevier Ltd. All rights reserved. |
DOI | 10.1016/j.neuroscience.2021.09.003 |
Type of Journal (Indian or Foreign) | Foreign |
Impact Factor (IF) | 3.590 |
Divison category:
Biochemical Sciences
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