Binding of AP-2 adaptor complex to brain membrane is regulated by phosphorylation of proteins
- Instituto de Histologia y Embriologia, Facultad de Ciencias Medicas, Universidad Nacional de Cuyo, Mendoza (5500) (Argentina)
Phosphorylation of proteins appears as a key process in early steps of clathrin coated vesicle formation. Here, we report that treatment of post-nuclear fraction with alkaline phosphatase induced redistribution of {alpha} subunits of AP-2 adaptor complex to cytosol and this effect was higher in the {alpha}2 subunit. A high serine phosphorylation status of {alpha} subunits correlated with the higher affinity of AP-2 to membranes. Using a simple binding assay, where membranes were incubated with either purified adaptors or cytosols, we observed an inhibitory effect of tyrphostin, a tyrosine kinase inhibitor, on the binding of AP-2 to membranes, but also an unexpected decrease induced by the phosphatase inhibitor cyclosporine. We also show an inhibitory effect of ATP mediated by cytosolic proteins, although it could not be related to the phosphorylation of AP-2, suggesting an action upstream a cascade of phosphorylations that participate in the regulation of the assembly of AP-2 to membranes.
- OSTI ID:
- 20709179
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 330, Issue 3; Other Information: DOI: 10.1016/j.bbrc.2005.03.038; PII: S0006-291X(05)00530-9; Copyright (c) 2005 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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