The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Pseudophosphorylation of tau at serine 422 inhibits caspase cleavage: in vitro evidence and implications for tangle formation in vivo
Abstract
The tangles of Alzheimer's disease (AD) are comprised of the tau protein displaying numerous alterations, including phosphorylation at serine 422 (S422) and truncation at aspartic acid 421 (D421). Truncation at the latter site appears to result from activation of caspases, a class of proteases that cleave specifically at aspartic acid residues. It has been proposed that phosphorylation at or near caspase cleavage sites could regulate the ability of the protease to cleave at those sites. Here, we use tau pseudophosphorylated at S422 (S422E) to examine the effects of tau phosphorylation on its cleavage by caspase 3. We find that S422E tau is more resistant to proteolysis by caspase 3 than non‐pseudophosphorylated tau. Additionally, we use antibodies directed against the phosphorylation site and against the truncation epitope to assess the presence of these epitopes in neurofibrillary tangles in the aged human brain. We show that phosphorylation precedes truncation during tangle maturation. Moreover, the distribution of the two epitopes suggests that a significant length of time (perhaps as much as two decades) elapses between S422 phosphorylation and cleavage at D421. We further conclude that tau phosphorylation at S422 may be a protective mechanism that inhibits cleavage in vivo.
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Cites
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Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology
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Reactivating Kinase/p38 Phosphorylates τ Protein In Vitro
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Inhibition of Tau Polymerization by Its Carboxy-Terminal Caspase Cleavage Fragment
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Tau in physiology and pathology
Wang, Y., & Mandelkow, E. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2015.1 · Cited by 2,251
Roles of tau protein in health and disease
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Tau protein kinases: Involvement in Alzheimer's disease
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Caspase activation precedes and leads to tangles
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Metadata
- Authors
- Guillozet‐Bongaarts, A. L., Cahill, M. E., Cryns, V. L., Reynolds, M. R., Berry, R. W., & Binder, L. I.
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2006-04-05
- Volume
- 97
- Issue
- 4
- Pages
- 1005-1014
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W2069620193
- Cited by
- 170
- References
- 7
- FWCI
- 4.31
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Pseudophosphorylation of tau at serine 422 inhibits caspase cleavage: in vitro evidence and implications for tangle formation in vivo. https://app.cochat.ai/papers/10.1111/j.1471-4159.2006.03784.x
- The paper
- Guillozet‐Bongaarts, A. L., Cahill, M. E., Cryns, V. L., Reynolds, M. R., Berry, R. W., & Binder, L. I. (2006). Pseudophosphorylation of tau at serine 422 inhibits caspase cleavage: in vitro evidence and implications for tangle formation in vivo. Journal of Neurochemistry. https://doi.org/10.1111/j.1471-4159.2006.03784.x
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