Dephosphorylation of distinct sites on microtubule-associated protein MAP1B by protein phosphatases 1, 2A and 2B

Luis Ulloa, Viktor Dombrádi, Javier Díaz-Nido, Kornélia Szücs, Pál Gergely, Peter Friedrich, Jesus Avila

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

Rat brain microtubule-associated protein MAP1 B has been tested as a substrate for Ser/Thr protein phosphatases (PP). The dephosphorylation reactions were followed by specific antibodies recognizing phosphorylated and phosphorylatable epitopes. One set of phosphorylation sites on MAPI B are referred to as mode I sites, and their phosphorylation is presumably catalyzed by proline-directed protein kinases. These mode I sites are efficiently dephosphorylated by PP2B and 2A but not by PP1. Another set of phosphorylation sites on MAP1B are named mode II sites, and their phosphorylation is possibly due to casein kinase II. These mode II sites are dephosphorylated by PP2A and PP1, the PP2B being ineffective. The selectivity of phosphatases for different sites within the same protein indicates the complexity of the dephosphorylation reactions regulating the functionality of MAP1B in neurons.

Original languageEnglish
Pages (from-to)85-89
Number of pages5
JournalFEBS letters
Volume330
Issue number1
DOIs
Publication statusPublished - Sep 6 1993

Keywords

  • CaScin kinase II (CKII)
  • Calcineurin
  • Microtubule-associated protein
  • Phosphorylation/dephosphorylation
  • Proline direct protein kinase (PDPK)
  • Protein phosphatase 1 and 2A

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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