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Polyamine Regulation of the Microtubule‐Associated Protein Kinase
Author(s) -
Nickerson Jeffrey A.,
Wells William W.
Publication year - 1986
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.1471-4159.1986.tb12932.x
Subject(s) - spermine , polyamine , phosphorylation , protein kinase a , microtubule , protein phosphorylation , biochemistry , kinase , chemistry , microbiology and biotechnology , biology , microtubule associated protein , enzyme
Microtubule protein prepared by cycles of assembly‐disassembly contains a cyclic AMP‐dependent protein kinase that phosphorylates the high‐molecular‐weight microtubule‐associated protein MAP‐2. The polyamine spermine at 2 m M affected the phosphorylation of MAP‐2 in a manner that depended on the cyclic AMP concentration. At cyclic AMP concentrations below 10 −6 M , spermine increased the rate of phosphorylation, while at cyclic AMP concentrations above 10 −6 M , spermine decreased the rate of phosphorylation. Spermine also decreased the final extent of cyclic AMP‐dependent phosphorylation but did not affect the protein substrate specificity of the microtubule‐associated protein kinase. MAP‐2 was the principal substrate both in the presence and in the absence of spermine. Because of these results, we propose that microtubule protein phosphorylation may be regulated in vivo by spermine as well as by cyclic AMP levels.