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Phosphorylation of Tubulin by Casein Kinase II Regulates Its Binding to a Neuronal Protein (NP185) Associated with Brain Coated Vesicles
Author(s) -
Kohtz D. Stave,
Puszkin Saul
Publication year - 1989
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1989.tb10929.x
Subject(s) - tubulin , casein kinase 2 , casein kinase 1 , cyclin dependent kinase 5 , phosphorylation , casein kinase 2, alpha 1 , biology , kinase , microbiology and biotechnology , protein phosphorylation , biochemistry , protein kinase a , neurite , cyclin dependent kinase 2 , chemistry , microtubule , in vitro
We recently described a new protein associated exclusively with neuronal clathrin‐coated vesicles (CCVs), and characterized two monoclonal antibodies that react with it (S‐8G8 and S‐6G7). In this report, the association of neuronal protein of 185 kilodaltons (NP185) with CCV kinases and its interaction with tubulin are described. The affinity of NP185 for tubulin is significantly enhanced when tubulin is phosphorylated by CCV‐associated casein kinase II. In contrast, phosphorylation of tubulin by a kinase activity associated with purified brain tubulin decreases its affinity for NP185. Together, these data suggest that the interaction of NP185 with tubulin is modulated by protein phosphorylation. Recent evidence has suggested that tubulin is phosphorylated by casein kinase II during neurite development. The enhanced affinity of NP185 for tubulin phosphorylated by casein kinase II could be important for proper intracellular sorting of this protein in the developing neuron.