Literature DB >> 6704120

MAP2 competes with MAP1 for binding to microtubules.

S A Kuznetsov, V I Rodionov, V I Gelfand, V A Rosenblat.   

Abstract

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.

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Year:  1984        PMID: 6704120     DOI: 10.1016/0006-291x(84)91635-8

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

1.  Differential interaction of synthetic peptides from the carboxyl-terminal regulatory domain of tubulin with microtubule-associated proteins.

Authors:  R B Maccioni; C I Rivas; J C Vera
Journal:  EMBO J       Date:  1988-07       Impact factor: 11.598

2.  Identification of a 34-kD polypeptide as a light chain of microtubule-associated protein-1 (MAP-1) and its association with a MAP-1 peptide that binds to microtubules.

Authors:  S A Kuznetsov; V I Rodionov; E S Nadezhdina; D B Murphy; V I Gelfand
Journal:  J Cell Biol       Date:  1986-03       Impact factor: 10.539

  2 in total

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