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...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 1998-08, Vol.281 (5378), p.821-824 |
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| creator | Slepnev, Vladimir I. Ochoa, Gian-Carlo Butler, Margaret H. Grabs, Detlev de Camilli, Pietro |
| description | 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. |
| doi_str_mv | 10.1126/science.281.5378.821 |
| format | Article |
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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.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.281.5378.821</identifier><identifier>PMID: 9694653</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Society for the Advancement of Science</publisher><subject>Adaptor Protein Complex alpha Subunits ; Adaptor Protein Complex beta Subunits ; Adaptor Proteins, Vesicular Transport ; Adenosine Triphosphate - metabolism ; Amino acids ; Animals ; Antibodies ; Binding Sites ; Biological and medical sciences ; Brain ; Carbazoles - pharmacology ; Cell physiology ; Cell receptors ; Chromatography, Affinity ; Clathrin ; Clathrin - metabolism ; Cyclosporine - pharmacology ; Cytosol ; Dimerization ; Dynamin I ; Dynamins ; Endocytosis ; Enzyme Inhibitors - pharmacology ; Fundamental and applied biological sciences. Psychology ; GTP Phosphohydrolases - metabolism ; Indole Alkaloids ; Membrane Proteins - metabolism ; Molecular and cellular biology ; Nerve Tissue Proteins - metabolism ; Nerves ; Nervous system ; Phosphatases ; Phosphoric Monoester Hydrolases - metabolism ; Phosphorylation ; Physiological aspects ; Physiological regulation ; Protein kinase inhibitors ; Proteins ; Rats ; Receptors ; Recombinant Fusion Proteins - metabolism ; Rodents ; src Homology Domains</subject><ispartof>Science (American Association for the Advancement of Science), 1998-08, Vol.281 (5378), p.821-824</ispartof><rights>Copyright 1998 American Association for the Advancement of Science</rights><rights>1998 INIST-CNRS</rights><rights>COPYRIGHT 1998 American Association for the Advancement of Science</rights><rights>COPYRIGHT 1998 American Association for the Advancement of Science</rights><rights>Copyright American Association for the Advancement of Science Aug 7, 1998</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c782t-ebfeb185f09ed67f418f144d83ee807437b3abc9066cba3fb579622ebe6a69373</citedby><cites>FETCH-LOGICAL-c782t-ebfeb185f09ed67f418f144d83ee807437b3abc9066cba3fb579622ebe6a69373</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2896222$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2896222$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,776,780,799,2871,2872,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2360723$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9694653$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Slepnev, Vladimir I.</creatorcontrib><creatorcontrib>Ochoa, Gian-Carlo</creatorcontrib><creatorcontrib>Butler, Margaret H.</creatorcontrib><creatorcontrib>Grabs, Detlev</creatorcontrib><creatorcontrib>de Camilli, Pietro</creatorcontrib><title>Role of Phosphorylation in Regulation of the Assembly of Endocytic Coat Complexes</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>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.</description><subject>Adaptor Protein Complex alpha Subunits</subject><subject>Adaptor Protein Complex beta Subunits</subject><subject>Adaptor Proteins, Vesicular Transport</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Brain</subject><subject>Carbazoles - pharmacology</subject><subject>Cell physiology</subject><subject>Cell receptors</subject><subject>Chromatography, Affinity</subject><subject>Clathrin</subject><subject>Clathrin - metabolism</subject><subject>Cyclosporine - pharmacology</subject><subject>Cytosol</subject><subject>Dimerization</subject><subject>Dynamin I</subject><subject>Dynamins</subject><subject>Endocytosis</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Fundamental and applied biological sciences. 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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.</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>9694653</pmid><doi>10.1126/science.281.5378.821</doi><tpages>4</tpages></addata></record> |
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| ispartof | Science (American Association for the Advancement of Science), 1998-08, Vol.281 (5378), p.821-824 |
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| language | eng |
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| source | American Association for the Advancement of Science; Jstor Complete Legacy; MEDLINE |
| subjects | Adaptor Protein Complex alpha Subunits Adaptor Protein Complex beta Subunits Adaptor Proteins, Vesicular Transport Adenosine Triphosphate - metabolism Amino acids Animals Antibodies Binding Sites Biological and medical sciences Brain Carbazoles - pharmacology Cell physiology Cell receptors Chromatography, Affinity Clathrin Clathrin - metabolism Cyclosporine - pharmacology Cytosol Dimerization Dynamin I Dynamins Endocytosis Enzyme Inhibitors - pharmacology Fundamental and applied biological sciences. Psychology GTP Phosphohydrolases - metabolism Indole Alkaloids Membrane Proteins - metabolism Molecular and cellular biology Nerve Tissue Proteins - metabolism Nerves Nervous system Phosphatases Phosphoric Monoester Hydrolases - metabolism Phosphorylation Physiological aspects Physiological regulation Protein kinase inhibitors Proteins Rats Receptors Recombinant Fusion Proteins - metabolism Rodents src Homology Domains |
| title | Role of Phosphorylation in Regulation of the Assembly of Endocytic Coat Complexes |
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