Gonda Y, Nishizawa K, Ando S, Kitamura S, Minoura Y, Nishi Y, Inagaki M
Laboratory of Experimental Radiology, Aichi Cancer Center Research Institute, Nagoya, Japan.
Biochem Biophys Res Commun. 1990 Mar 30;167(3):1316-25. doi: 10.1016/0006-291x(90)90667-c.
Protein kinase C phosphorylated the major mammalian neurofilament protein (NF-L) with approximately 3 mol phosphate per mol protein. The phosphorylated NF-L no longer formed the filaments. Sequential analysis of the tryptic phosphopeptides, together with the known primary sequence, revealed that Ser-12, Ser-27, Ser-33 and Ser-51 were phosphorylated by protein kinase C. These findings contribute toward elucidation of mechanisms regulating the functions of neurofilaments.
蛋白激酶C使主要的哺乳动物神经丝蛋白（NF-L）磷酸化，每摩尔蛋白约含3摩尔磷酸。磷酸化的NF-L不再形成细丝。对胰蛋白酶磷酸肽的序列分析以及已知的一级序列表明，丝氨酸-12、丝氨酸-27、丝氨酸-33和丝氨酸-51被蛋白激酶C磷酸化。这些发现有助于阐明调节神经丝功能的机制。
