Phosphorylation and dephosphorylation in the proline-rich C-terminal domain of microtubule-associated protein 2

Carlos Sánchez, Peter Tompa, Kornélia Szücs, Peter Friedrich, Jesús Avila

Research output: Article

52 Citations (Scopus)

Abstract

The C-terminal domain of microtubule-associated protein 2 (MAP2) contains a proline-rich region and the tubulin-binding domain. We have generated antibodies to follow the phosphorylation state of the proline-rich domain. One of these antibodies (no. 305) has been raised against a synthetic peptide P (sequence RTPGTPGTPSY) phosphorylated at the threonine residues. This sequence is present in the proline-rich region of MAP2 and is phosphorylated in vitro by at least three different proline-directed protein kinases: p42(mpk), p34(cdc2), and GSK3 (glycogen-synthase kinase 3) α/β. The MAP2 sites phosphorylated by these kinases are different, although all of them phosphorylate the C-terminal domain of MAP2 as determined by Staphylococcus aureus V8 protease mapping. Nonphosphorylated peptide P can be phosphorylated in vitro by all three kinases studied with similar efficiency. In high-molecular-mass MAP2, this sequence is highly phosphorylated in vivo at the late stages of rat development. This motif can be rapidly dephosphorylated in vitro by protein-phosphatase 1 (PP1) and 2A (PP2A) catalytic subunits but not by PP2B.

Original languageEnglish
Pages (from-to)765-771
Number of pages7
JournalEuropean Journal of Biochemistry
Volume241
Issue number3
DOIs
Publication statusPublished - 1996

ASJC Scopus subject areas

  • Biochemistry

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