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PINCH in the cellular stress response to tau-hyperphosphorylation.

PloS one | 2013

Particularly interesting new cysteine- histidine- rich protein (PINCH) is an adaptor protein that our data have shown is required for neurite extension under stressful conditions. Our previous studies also report that PINCH is recalled by neurons showing decreased levels of synaptodendritic signaling proteins such as MAP2 or synaptophysin in the brains of human immunodeficiency virus (HIV) patients. The current study addressed potential role(s) for PINCH in neurodegenerative diseases. Mass spectrometry predicted the interaction of PINCH with Tau and with members of the heat shock response. Our in vitro data confirmed that PINCH binds to hyperphosphorylated (hp) Tau and to E3 ubiquitin ligase, carboxy-terminus of heat shock-70 interacting protein. Silencing PINCH prior to induction of hp-Tau resulted in more efficient clearance of accumulating hp-Tau, suggesting that PINCH may play a role in stabilizing hp-Tau. Accumulation of hp-Tau is implicated in more than 20 neuropathological diseases including Alzheimer's disease (AD), frontotemporal dementia (FTD), and human immunodeficiency virus encephalitis (HIVE). Analyses of brain tissues from HIVE, AD and FTD patients showed that PINCH is increased and binds to hp-Tau. These studies address a new mechanism by which AD and HIV may intersect and identify PINCH as a contributing factor to the accumulation of hyperphosphorylated Tau.

Pubmed ID: 23554879 RIS Download

Research resources used in this publication

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Associated grants

  • Agency: NIMH NIH HHS, United States
    Id: R01 MH107340
  • Agency: NIMH NIH HHS, United States
    Id: U24 MH100928
  • Agency: NIMH NIH HHS, United States
    Id: R01 MH085602
  • Agency: NIMH NIH HHS, United States
    Id: U01 MH083506
  • Agency: NIMH NIH HHS, United States
    Id: P30 MH092177
  • Agency: NIMH NIH HHS, United States
    Id: R01-MH085602

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