Microtubule dynamics.
Although compelling evidence has been obtained for heterogeneity in the structure of subunits in microtubules, it has not been possible to prove that this results from the presence of tubulin-GDP and tubulin-GTP in polymers. There are reasons to exclude the existence of even a monolayer of tubulin-GTP subunits at microtubule ends. Dynamic behavior appears to be best accounted for by a mechanism in which tubulin-GDP in microtubules exists in two conformations. The mechanism of microtubule-associated protein binding to microtubules and the role of phosphorylation on this reaction are discussed.
Caplow
M
M
Department of Biochemistry, University of North Carolina, Chapel Hill 27599-7260.
D000818:Animals; D006153:Guanosine Diphosphate / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D008869:Microtubule-Associated Proteins / Q000502:physiology; D008870:Microtubules / Q000378:metabolism*; D010766:Phosphorylation; D014404:Tubulin / Q000378:metabolism
D008869:Microtubule-Associated Proteins; D014404:Tubulin; D006153:Guanosine Diphosphate; D006160:Guanosine Triphosphate