Premium
Dephosphorylation of distinct sites on microtubule‐associated protein MAP1B by protein phosphatases 1, 2A and 2B
Author(s) -
Ulloa Luis,
Dombrádi Viktor,
Díaz-Nido Javier,
Szücs Kornélia,
Gergely Pál,
Friedrich Peter,
Avila Jesus
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80925-k
Subject(s) - dephosphorylation , phosphorylation , phosphatase , protein phosphorylation , kinase , protein phosphatase 2 , protein kinase a , biochemistry , chemistry , microbiology and biotechnology , biology
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.