Role of phosphorylation in regulation of the assembly of endocytic coat complexes.
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.
Mesh Terms:
Adaptor Protein Complex alpha Subunits, Adaptor Protein Complex beta Subunits, Adaptor Proteins, Vesicular Transport, Adenosine Triphosphate, Animals, Binding Sites, Carbazoles, Chromatography, Affinity, Clathrin, Cyclosporine, Dimerization, Dynamin I, Dynamins, Endocytosis, Enzyme Inhibitors, GTP Phosphohydrolases, Indole Alkaloids, Membrane Proteins, Nerve Tissue Proteins, Phosphoric Monoester Hydrolases, Rats, Recombinant Fusion Proteins, src Homology Domains
Adaptor Protein Complex alpha Subunits, Adaptor Protein Complex beta Subunits, Adaptor Proteins, Vesicular Transport, Adenosine Triphosphate, Animals, Binding Sites, Carbazoles, Chromatography, Affinity, Clathrin, Cyclosporine, Dimerization, Dynamin I, Dynamins, Endocytosis, Enzyme Inhibitors, GTP Phosphohydrolases, Indole Alkaloids, Membrane Proteins, Nerve Tissue Proteins, Phosphoric Monoester Hydrolases, Rats, Recombinant Fusion Proteins, src Homology Domains
Science
Date: Aug. 07, 1998
PubMed ID: 9694653
View in: Pubmed Google Scholar
Download Curated Data For This Publication
9400
Switch View:
- Interactions 1