A microtubule-associated protein (MAP2) kinase restores microtubule motility in embryonic brain

Luis A. López, Michael Sheetz

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

Motility driven by the microtubule motors, kinesin and cytoplasmic dynein, is inhibited by MAP2 (Lopez, L. A., and Sheetz, M. P. (1993) Cell Motil. Cytoskeleton 24, 1-16). The MAP2 inhibition is reversed by a kinase that is co-purified with chicken embryonic MAP2, completely releasing MAP2 from the microtubules. We have identified this activity with a kinase, embryonic MAP2 kinase (M(r) = 100,000), which phosphorylates MAP2 at serine amino acid residues. This kinase is c-AMP independent and inhibited by potassium fluoride and glycerol 2-phosphate. Only the phosphorylation produced by embryonic MAP2 kinase can change the affinity of MAP2 by microtubules. Bovine MAP2 kinase, Cdc2 kinase, mitogenic activated protein kinase, and the NIMA kinase are able to phosphorylate MAP2 but do not change the affinity for microtubules. In vivo, embryonic MAP2 kinase could play a major role in the regulation of motility and positioning of membranous organelles within the cells even at substoichiometric levels.

Original languageEnglish (US)
Pages (from-to)12511-12517
Number of pages7
JournalJournal of Biological Chemistry
Volume270
Issue number21
DOIs
StatePublished - May 26 1995
Externally publishedYes

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Microtubule-Associated Proteins
Microtubules
Protein Kinases
Brain
Phosphotransferases
Cytoplasmic Dyneins
Kinesin
Phosphorylation
Adenosine Monophosphate
Cytoskeleton
Organelles
Glycerol
Serine
Chickens
Phosphates
Amino Acids

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

A microtubule-associated protein (MAP2) kinase restores microtubule motility in embryonic brain. / López, Luis A.; Sheetz, Michael.

In: Journal of Biological Chemistry, Vol. 270, No. 21, 26.05.1995, p. 12511-12517.

Research output: Contribution to journalArticle

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