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Phosphorylation of human microtubule‐associated protein tau by protein kinases of the AGC subfamily
Author(s) -
Virdee Kanwar,
Yoshida Hirotaka,
Peak-Chew Sew,
Goedert Michel
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.05.009
Subject(s) - phosphorylation , kinase , biology , subfamily , microtubule , microbiology and biotechnology , tau protein , genetics , gene , alzheimer's disease , medicine , disease , pathology
Intraneuronal inclusions made of hyperphosphorylated microtubule‐associated protein tau are a defining neuropathological characteristic of Alzheimer's disease, and of several other neurodegenerative disorders. Many phosphorylation sites in tau are S/TP sites that flank the microtubule‐binding repeats. Others are KXGS motifs in the repeats. One site upstream of the repeats lies in a consensus sequence for AGC kinases. This site (S214) is believed to play an important role in the events leading from normal, soluble to filamentous, insoluble tau. Here, we show that all AGC kinases tested phosphorylated S214. RSK1 and p70 S6 kinase also phosphorylated the neighbouring T212, a TP site that conforms weakly to the AGC kinase consensus sequence. MSK1 phosphorylated S214, as well as S262, a KXGS site in the first repeat, and S305 in the second repeat.