Identification of actin kinase activity in purified fragmin-actin complex.
Actin kinase phosphorylates actin of fragmin-actin complex, resulting in the inactivation of the nucleation and capping activities of the complex. Fragmin-actin complex was prepared by a new purification procedure. Incubation with ATP caused inactivation of the purified complex and phosphorylation of actin of fragmin-actin complex. The detailed analysis of the complex by SDS-gel electrophoresis showed that actin kinase was co-purified with the fragmin-actin complex. Formation of such an association between actin kinase and substrate suggests that the kinase is localized on the fragmin-actin complex to efficiently regulate actin cytoskeletons.
Furuhashi
K
K
Department of Molecular Biology, School of Science, Nagoya University, Japan.
Hatano
S
S
D000199:Actins / Q000302:isolation & purification / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D002853:Chromatography, Liquid; D003599:Cytoskeleton / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006495:Heparin, Low-Molecular-Weight / Q000302:isolation & purification / Q000378:metabolism*; D009132:Muscles / Q000201:enzymology / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases
D000199:Actins; D006495:Heparin, Low-Molecular-Weight; D000255:Adenosine Triphosphate; D011494:Protein Kinases; C074377:actin kinase; D017346:Protein Serine-Threonine Kinases