Concerning the anomalous kinetic behavior of microtubules.
We have demonstrated that tubulin-GTP subunits can react with microtubule ends containing subunits with E-site-bound GDP. This observation can be taken to rule out a previous interpretation of a biphasic dependence of the rate for subunit flux into microtubules on the subunit concentration, which is based upon an assumption that GTP is required to be present in subunits at microtubule ends in order to allow addition of tubulin-GTP subunits. The nullified mechanism had been suggested to be the basis of the observation that growing and shrinking microtubules coexist as independent species. We have also confirmed previous studies indicating that the flux rate is nonlinearly dependent on the subunit concentration and account for this behavior by assuming that tubulin-GTP subunits reversibly add to microtubule ends by two paths. In one, tubulin-GTP subunits add nonproductively to generate an end which is unable to undergo further net microtubule elongation; however, this reaction can retard the rate for microtubule disassembly under conditions where the disassembly reaction predominates. In the other, tubulin-GTP subunits add productively to microtubule ends to generate ends which can undergo subsequent net elongation.
D000818:Animals; D004121:Dimethyl Sulfoxide / Q000494:pharmacology; D020558:GTP Phosphohydrolases / Q000378:metabolism; D006150:Guanine Nucleotides / Q000378:metabolism*; D006153:Guanosine Diphosphate / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000378:metabolism*; D007700:Kinetics; D008870:Microtubules / Q000187:drug effects / Q000378:metabolism*; D013552:Swine; D014404:Tubulin / Q000378:metabolism*
D006150:Guanine Nucleotides; D014404:Tubulin; D006153:Guanosine Diphosphate; D006160:Guanosine Triphosphate; D020558:GTP Phosphohydrolases; D004121:Dimethyl Sulfoxide