Role of Phosphorylation in Regulation of the Assembly of Endocytic Coat Complexes
| Autor: | Detlev Grabs, Gian-Carlo Ochoa, Margaret H. Butler, Vladimir I. Slepnev, Pietro De Camilli |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
Dynamins
Recombinant Fusion Proteins Endocytic cycle Carbazoles Nerve Tissue Proteins Synaptojanin Biology Endocytosis Clathrin coat Clathrin Chromatography Affinity GTP Phosphohydrolases Indole Alkaloids src Homology Domains Adaptor Protein Complex alpha Subunits Adenosine Triphosphate Animals Adaptor Protein Complex beta Subunits Enzyme Inhibitors Dynamin I Dynamin Synaptic vesicle endocytosis Binding Sites Multidisciplinary Membrane Proteins Phosphoric Monoester Hydrolases Rats Cell biology Adaptor Proteins Vesicular Transport Amphiphysin Cyclosporine biology.protein Dimerization |
| Zdroj: | Science. 281:821-824 |
| ISSN: | 1095-9203 0036-8075 |
| DOI: | 10.1126/science.281.5378.821 |
| Popis: | Clathrin-mediated endocytosis involves cycles of assembly and disassembly of clathrin coat components and their accessory proteins. Dephosphorylation of rat brain extract was shown to promote the assembly of dynamin 1, synaptojanin 1, and amphiphysin into complexes that also included clathrin and AP-2. Phosphorylation of dynamin 1 and synaptojanin 1 inhibited their binding to amphiphysin, whereas phosphorylation of amphiphysin inhibited its binding to AP-2 and clathrin. Thus, phosphorylation regulates the association and dissociation cycle of the clathrin-based endocytic machinery, and calcium-dependent dephosphorylation of endocytic proteins could prepare nerve terminals for a burst of endocytosis. |
| Databáze: | OpenAIRE |
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