Mapmodulin: a possible modulator of the interaction of microtubule-associated proteins with microtubules

Proc Natl Acad Sci U S A. 1997 May 13;94(10):5084-9. doi: 10.1073/pnas.94.10.5084.

Abstract

We have purified and characterized a 31-kDa protein named mapmodulin that binds to the microtubule-associated proteins (MAPs) MAP2, MAP4, and tau. Mapmodulin binds free MAPs in strong preference to microtubule-associated MAPs, and appears to do so via the MAP's tubulin-binding domain. Mapmodulin inhibits the initial rate of MAP2 binding to microtubules, a property that may allow mapmodulin to displace MAPs from the path of organelles translocating along microtubules. In support of this possibility, mapmodulin stimulates the microtubule- and dynein-dependent localization of Golgi complexes in semi-intact CHO cells. To our knowledge, mapmodulin represents the first example of a protein that can bind and potentially regulate multiple MAP proteins.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • CHO Cells
  • Chromatography, Gel
  • Cricetinae
  • Cytosol
  • Dyneins / chemistry
  • Dyneins / physiology
  • Golgi Apparatus / physiology
  • Intracellular Membranes / physiology
  • Intracellular Signaling Peptides and Proteins
  • Kinetics
  • Microtubule-Associated Proteins / chemistry
  • Microtubule-Associated Proteins / isolation & purification
  • Microtubule-Associated Proteins / physiology*
  • Microtubules / physiology*
  • Microtubules / ultrastructure
  • Models, Structural
  • Nuclear Proteins
  • Peptide Fragments / chemistry
  • Protein Binding
  • Proteins / chemistry
  • Proteins / isolation & purification
  • Proteins / physiology*
  • RNA-Binding Proteins

Substances

  • ANP32A protein, human
  • Intracellular Signaling Peptides and Proteins
  • Microtubule-Associated Proteins
  • Nuclear Proteins
  • Peptide Fragments
  • Proteins
  • RNA-Binding Proteins
  • Dyneins