MAP2 competes with MAP1 for binding to microtubules.
A question whether MAP1 and MAP2 (the major microtubule associated proteins from mammalian brain) bind to common or distinct sites on the microtubule surface was studied. Microtubules were assembled from tubulin and MAP1 and then centrifuged through a layer of MAP2 solution under conditions where no repolymerization of tubulin with MAP2 could occur. During centrifugation, MAP2 displaced most of MAP1 on the microtubules. This implies that MAP1 is reversibly bound to microtubules and that MAP2 binding interferes with MAP1 binding. The latter means that binding sites for MAP1 and MAP2 are identical or overlap.
D000818:Animals; D001667:Binding, Competitive; D002417:Cattle; D002498:Centrifugation; D006160:Guanosine Triphosphate / Q000494:pharmacology; D046911:Macromolecular Substances; D008869:Microtubule-Associated Proteins; D008870:Microtubules / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism*; D014404:Tubulin / Q000378:metabolism
D046911:Macromolecular Substances; D008869:Microtubule-Associated Proteins; D011506:Proteins; D014404:Tubulin; D006160:Guanosine Triphosphate