Premium
Tau tubulin kinases in proteinopathy
Author(s) -
Taylor Laura M.,
McMillan Pamela J.,
Kraemer Brian C.,
Liachko Nicole F.
Publication year - 2019
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.14866
Subject(s) - neurodegeneration , amyotrophic lateral sclerosis , frontotemporal dementia , neuroscience , frontotemporal lobar degeneration , disease , phosphorylation , corticobasal degeneration , kinase , dementia , neurotoxicity , biology , medicine , pathology , microbiology and biotechnology , toxicity
A number of neurodegenerative diseases are characterized by deposition of abnormally phosphorylated tau or TDP ‐43 in disease‐affected neurons. These diseases include Alzheimer's disease, frontotemporal lobar degeneration, and amyotrophic lateral sclerosis. No disease‐modifying therapeutics is available to treat these disorders, and we have a limited understanding of the cellular and molecular factors integral to disease initiation or progression. Phosphorylated tau and TDP ‐43 are important markers of pathology in dementia disorders and directly contribute to tau‐ and TDP ‐43‐related neurotoxicity and neurodegeneration. Here, we review the scope of tau and TDP ‐43 phosphorylation in neurodegenerative disease and discuss recent work demonstrating the kinases TTBK 1 and TTBK 2 phosphorylate both tau and TDP ‐43, promoting neurodegeneration.