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Caspase-2 and tau—a toxic partnership?

Nature Medicine volume 22, pages 1207–1208 (2016)Cite this article

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Misfolded and hyperphosphorylated forms of the microtubule-associated protein tau are thought to be responsible for some degree of neurodegeneration. The demonstration of a novel toxic cleavage of tau by caspase-2 opens up new therapeutic avenues.

Under physiological conditions, the microtubule-associated protein tau1 is confined largely to neurons, and more specifically, to their axons2. Its normal function is to promote microtubule assembly and stability3. In Alzheimer's disease (AD), there is abnormal phosphorylation and aggregation of tau4, which leads to the formation of paired helical filaments (PHFs)5,6, which form the neurofibrillary tangles that are a hallmark of AD. Identical tangles are formed in fronto-temporal dementia (FTD) and other tauopathies7.

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Figure 1: Caspase-2 cleavage of tau.

Katie Vicari/Nature Publishing Group

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Authors and Affiliations

  1. Department of Pathology and Cell Biology, Carol M. Troy and Michael L. Shelanski are at the Taub Institute for Research on Alzheimer's Disease and the Aging Brain, Columbia University, New York, New York, USA.,

    Carol M Troy & Michael L Shelanski

  2. Carol M. Troy is also in the Department of Neurology.,

    Carol M Troy

Authors
  1. Carol M Troy
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  2. Michael L Shelanski
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Correspondence to Michael L Shelanski.

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The authors declare no competing financial interests.

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Troy, C., Shelanski, M. Caspase-2 and tau—a toxic partnership?. Nat Med 22, 1207–1208 (2016). https://doi.org/10.1038/nm.4227

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