Differential phosphorylation of microtubule proteins by ATP and GTP.
Purified brain microtubule protein is phosphorylated by endogenous protein kinase activities in the presence of [gamma-32P] ATP or [gamma-32P] GTP. Here we show that certain microtubule-associated proteins are phosphorylated differently by GTP or ATP as direct phosphoryl donors, suggesting the presence of distinct kinase activities, with different specificities, associated with microtubule protein.
Diaz-Nido
J
J
Centro de Biología Molecular (CSIC-UAM), Universidad Autónoma, Madrid, Spain.
Serrano
L
L
Avila
J
J
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D006160:Guanosine Triphosphate / Q000378:metabolism*; D008868:Microtubule Proteins / Q000378:metabolism*; D010449:Peptide Mapping; D010766:Phosphorylation; D013552:Swine
D008868:Microtubule Proteins; D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate