Aurora A on the mitotic spindle is activated by the way it holds its partner.
An exciting study in this issue reveals how binding of the microtubule associated protein TPX2 to the mitotic kinase Aurora A induces a conformational change. This moves the phosphorylated activation domain into a more compact position within the kinase core, providing a better substrate binding platform and hiding the activating phosphoryl group from attack by PP1.
Glover
David M
DM
Cancer Research UK Cell Cycle Genetics Research Group, University of Cambridge, Department of Genetics, Downing Street, Cambridge CB2 3EH, United Kingdom.
D000818:Animals; D064127:Aurora Kinases; D018797:Cell Cycle Proteins; D006801:Humans; D008869:Microtubule-Associated Proteins / Q000502:physiology*; D008938:Mitosis / Q000502:physiology*; D009363:Neoplasm Proteins; D009687:Nuclear Proteins; D010750:Phosphoproteins; D011485:Protein Binding / Q000502:physiology; D011494:Protein Kinases / Q000502:physiology*; D017346:Protein Serine-Threonine Kinases; D017434:Protein Structure, Tertiary / Q000502:physiology; D008941:Spindle Apparatus / Q000201:enzymology*; D029867:Xenopus Proteins
D018797:Cell Cycle Proteins; D008869:Microtubule-Associated Proteins; D009363:Neoplasm Proteins; D009687:Nuclear Proteins; D010750:Phosphoproteins; C122167:TPX2 protein, human; D029867:Xenopus Proteins; D011494:Protein Kinases; C112134:AURKA protein, Xenopus; D064127:Aurora Kinases; D017346:Protein Serine-Threonine Kinases