Title | Phosphorylation and dephosphorylation in the proline-rich C-terminal domain of microtubule-associated protein 2. |
Publication Type | Journal Article |
Year of Publication | 1996 |
Authors | Sánchez, C., P. Tompa, K. Szücs, P. Friedrich, and J. Avila |
Journal | Eur J Biochem |
Volume | 241 |
Issue | 3 |
Pagination | 765-71 |
Date Published | 1996 Nov 1 |
ISSN | 0014-2956 |
Keywords | Animals, Antibodies, Antibody Specificity, Brain Chemistry, Epitopes, Microtubule-Associated Proteins, Oligopeptides, Phosphoprotein Phosphatases, Phosphorylation, Proline, Proline-Directed Protein Kinases, Protein Phosphatase 1, Protein-Serine-Threonine Kinases, Rats |
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: p42mpk, p34cdc2, and GSK3 (glycogen-synthase kinase 3) alpha/beta. 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. |
Alternate Journal | Eur. J. Biochem. |
PubMed ID | 8944764 |
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