beta2-adaptin is constitutively de-phosphorylated by serine/threonine protein phosphatase PP2A and phosphorylated by a staurosporine-sensitive kinase
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beta2-adaptin is constitutively de-phosphorylated by serine/threonine protein phosphatase PP2A and phosphorylated by a staurosporine-sensitive kinase. / Lauritsen, Jens Peter Holst; Menné, C; Kastrup, J; Dietrich, J; Odum, Niels; Geisler, C.
In: BBA General Subjects, Vol. 1497, No. 3, 2000, p. 297-307.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - beta2-adaptin is constitutively de-phosphorylated by serine/threonine protein phosphatase PP2A and phosphorylated by a staurosporine-sensitive kinase
AU - Lauritsen, Jens Peter Holst
AU - Menné, C
AU - Kastrup, J
AU - Dietrich, J
AU - Odum, Niels
AU - Geisler, C
N1 - 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
PY - 2000
Y1 - 2000
N2 - 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.
AB - 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.
M3 - Journal article
C2 - 10996654
VL - 1497
SP - 297
EP - 307
JO - B B A - General Subjects
JF - B B A - General Subjects
SN - 0304-4165
IS - 3
ER -
ID: 8544905