@article{9f44eaa0b0a111ddb538000ea68e967b,
title = "beta2-adaptin is constitutively de-phosphorylated by serine/threonine protein phosphatase PP2A and phosphorylated by a staurosporine-sensitive kinase",
abstract = "Clathrin-mediated endocytosis includes cycles of assembly and disassembly of the clathrin-coated vesicle constituents. How these cycles are regulated is still not fully known but previous studies have indicated that phosphorylation of coat subunits may play a role. Here we describe that beta2-adaptin undergoes cycles of phosphorylation/de-phosphorylation in intact cells. Thus, beta2-adaptin was constitutively de-phosphorylated by serine/threonine protein phosphatase 2A and phosphorylated by a staurosporine-sensitive kinase in vivo. Confocal laser scanning microscopy demonstrated that phosphorylated AP2 complexes were found more evenly distributed at the plasma membrane compared to non-phosphorylated AP2 complexes which were found in aggregates. Finally, we found that phosphorylation of beta2-adaptin correlated with inhibition of clathrin-mediated endocytosis. Our results support the hypothesis that phosphorylation/de-phosphorylation of coat proteins plays a regulatory role in the assembly/disassembly cycle of clathrin-coated vesicles.",
author = "Lauritsen, {Jens Peter Holst} and C Menn{\'e} and J Kastrup and J Dietrich and Niels Odum and C Geisler",
note = "Keywords: Adaptor Protein Complex beta Subunits; Antibiotics, Antifungal; Cell Membrane; Cells, Cultured; Endocytosis; Enzyme Inhibitors; Humans; Jurkat Cells; Membrane Proteins; Microscopy, Confocal; Okadaic Acid; Oxazoles; Phosphoprotein Phosphatases; Phosphorylation; Protein Kinases; Protein Phosphatase 2; Pyrans; Spiro Compounds; Staurosporine",
year = "2000",
language = "English",
volume = "1497",
pages = "297--307",
journal = "B B A - General Subjects",
issn = "0304-4165",
publisher = "Elsevier",
number = "3",
}