The molecular implications of a caspase-2-mediated site-specific tau cleavage in tauopathies
Peng Liu1
Karen H.Ashe2
1.Department of Neurology, University of Minnesota,Minneapolis, MN, USA;N.Bud Grossman Center for Memory Research and Care, University of Minnesota, Minneapolis,MN, USA2.Department of Neurology, University of Minnesota,Minneapolis, MN, USA;Department of Neuroscience, University of Minnesota, Minneapolis, MN, USA;N.Bud Grossman Center for Memory Research and Care, University of Minnesota, Minneapolis,MN, USA;Geriatric Research, Education, and Clinical Centers,Veterans Affairs Medical Center, Minneapolis, MN,USA
摘要：A major focus of current experimental therapies for neurodegenerative diseases is on modulating post-translational modifications(PTMs)of the microtubule-associated protein tau.Tau is a highly soluble,neuronal protein that is comprised of four domains-the N-terminal projection domain,the proline-rich region,the microtubule-binding domain,and the C-terminal tail.As a scaffold protein,tau dynamically interacts with numerous structural and functional biomolecules,such as cytoskeleton and motor proteins,chaperones,enzymes,DNA,RNA,and lipids.Over a dozen types of PTMs,combined with alternative splicing,confer upon tau its enormous structural heterogeneity,which subserves its many(patho-)physiological functions.
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论文发表日期：2021-09-28
在线出版日期：2025-08-15（本平台首次上网日期，不代表文献的发表时间）
页数：2( 1774-1775 )