Ishiguro K, Omori A, Sato K, Tomizawa K, Imahori K, Uchida T
Mitsubishi Kasei Institute of Life Sciences, Tokyo, Japan.
Neurosci Lett. 1991 Jul 22;128(2):195-8. doi: 10.1016/0304-3940(91)90259-v.
Previously we partially purified a novel protein kinase which phosphorylated tau and formed a paired helical filament (PHF) epitope. In this paper we show that the kinase fraction contains a protein kinase activity recognizing serine/threonine proline sequence. The kinase phosphorylated tau at the tau-1 site previously reported as one of the phosphorylation sites on PHF by other groups. The kinase also phosphorylated extraordinarily insoluble portion located on C-terminal region of tau in PHF. It is worth considering that tau phosphorylated by this kinase activity is incorporated into PHF.
此前，我们部分纯化了一种新型蛋白激酶，该激酶可使tau蛋白磷酸化并形成双螺旋丝（PHF）表位。在本文中，我们表明该激酶组分含有一种识别丝氨酸/苏氨酸 - 脯氨酸序列的蛋白激酶活性。该激酶在tau - 1位点使tau蛋白磷酸化，tau - 1位点先前被其他研究小组报道为PHF上的磷酸化位点之一。该激酶还使位于PHF中tau蛋白C末端区域的极难溶解部分磷酸化。值得考虑的是，被这种激酶活性磷酸化的tau蛋白会整合到PHF中。
