Work

Dephosphorylation of microtubule‐associated protein tau by protein phosphatase‐1 and ‐2C and its implication in Alzheimer disease

Year: 1994

Type: article

Abstract: Microtubule-associated protein tau is abnormally hyperphosphorylated and forms the major protein subunit of paired helical filaments (PHF) in Alzheimer disease brains. The abnormally phosphorylated sites Ser-199, Ser-202, Ser-396 and Ser-404 but not Ser-46 and Ser-235 of Alzheimer tau were found to be dephosphorylated by protein phosphatase-1 and this dephosphorylation was activated by Mn2+. In contrast, protein phosphatase-2C did not dephosphorylate any of these sites. Both protein phosphatase-1 and -2C had high activities towards [32P]tau phosphorylated by cAMP-dependent protein kinase. These results suggest that both protein phosphatase-1 and -2C might be associated with normal phosphorylation state of tau, but only the former and not the latter phosphatase is involved in its abnormal phosphorylation in Alzheimer disease.

Source: FEBS Letters

DOI: 10.1016/0014-5793(94)80247-5

Authors: Cheng-Xin Gong, Inge Grundke-Iqbal, Zahi Damuni, Khalid Iqbal

Institutions: Pennsylvania State University, Penn State Milton S. Hershey Medical Center

Language: English

Topic: Alzheimer's disease research and treatments

Subfield: Physiology

Field: Medicine

Domain: Health Sciences

SDG: Good health and well-being

Open Access status: bronze

Funders: National Institutes of Health, National Institute on Aging, National Institute of Neurological Disorders and Stroke