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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5378
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pubmed:dateCreated |
1998-8-14
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pubmed:abstractText |
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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Protein Complex alpha...,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Protein Complex beta...,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Vesicular...,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Carbazoles,
http://linkedlifedata.com/resource/pubmed/chemical/Clathrin,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclosporine,
http://linkedlifedata.com/resource/pubmed/chemical/Dynamin I,
http://linkedlifedata.com/resource/pubmed/chemical/Dynamins,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Indole Alkaloids,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Monoester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/amphiphysin,
http://linkedlifedata.com/resource/pubmed/chemical/staurosporine aglycone,
http://linkedlifedata.com/resource/pubmed/chemical/synaptojanin
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
281
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
821-4
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:9694653-Adaptor Protein Complex alpha Subunits,
pubmed-meshheading:9694653-Adaptor Protein Complex beta Subunits,
pubmed-meshheading:9694653-Adaptor Proteins, Vesicular Transport,
pubmed-meshheading:9694653-Adenosine Triphosphate,
pubmed-meshheading:9694653-Animals,
pubmed-meshheading:9694653-Binding Sites,
pubmed-meshheading:9694653-Carbazoles,
pubmed-meshheading:9694653-Chromatography, Affinity,
pubmed-meshheading:9694653-Clathrin,
pubmed-meshheading:9694653-Cyclosporine,
pubmed-meshheading:9694653-Dimerization,
pubmed-meshheading:9694653-Dynamin I,
pubmed-meshheading:9694653-Dynamins,
pubmed-meshheading:9694653-Endocytosis,
pubmed-meshheading:9694653-Enzyme Inhibitors,
pubmed-meshheading:9694653-GTP Phosphohydrolases,
pubmed-meshheading:9694653-Indole Alkaloids,
pubmed-meshheading:9694653-Membrane Proteins,
pubmed-meshheading:9694653-Nerve Tissue Proteins,
pubmed-meshheading:9694653-Phosphoric Monoester Hydrolases,
pubmed-meshheading:9694653-Rats,
pubmed-meshheading:9694653-Recombinant Fusion Proteins,
pubmed-meshheading:9694653-src Homology Domains
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pubmed:year |
1998
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pubmed:articleTitle |
Role of phosphorylation in regulation of the assembly of endocytic coat complexes.
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pubmed:affiliation |
Howard Hughes Medical Institute and Department of Cell Biology, Yale University School of Medicine, 295 Congress Avenue, New Haven, CT 06510, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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