4.6 Article

Regulation of GSK3 isoforms by phosphatases PP1 and PP2A

Journal

MOLECULAR AND CELLULAR BIOCHEMISTRY
Volume 344, Issue 1-2, Pages 211-215

Publisher

SPRINGER
DOI: 10.1007/s11010-010-0544-0

Keywords

GSK-3; PP1; PP2A; Okadaic acid; Lithium

Categories

Funding

  1. Comunidad de Madrid (NEURODEGMODELS-CM)
  2. Spanish Comision Interministerial de Ciencia y Tecnologia
  3. Fundacion Centro Investigacion Enfermedades Neurologicas (Fundacion CIEN)
  4. CIBER
  5. Fundacion Ramon Areces

Ask authors/readers for more resources

Dephosphorylation of phospho GSK3 isoforms, from COS-7 cells, was determined in vitro and in cultured cells in the absence or the presence of okadaic acid and lithium. Our results indicate a preferential dephosphorylation of phospho GSK3 alpha by PP2A phosphatase, whereas dephosphorylation of phospho GSK3 beta mainly takes place by PP1 phosphatase.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.6
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available