Receptor and protein kinase C-mediated regulation of ARF binding to the Golgi complex
THE formation of constitutive transport vesicles involves the association of non-clathrin coat proteins to transport organelles 1,2 . Here we report that IgE receptors and protein kinase C (PKC) regulate the GTP-dependent binding of the two coat proteins ADP-ribosylation factor (ARF) and β -COP 3–5...
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| Veröffentlicht in: | Nature (London) 1993-08, Vol.364 (6440), p.818-821 |
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| creator | De Matteis, Maria Antonietta Santini, Giovanna Kahn, Richard A. Di Tullio, Giuseppe Luini, Alberto |
| description | THE formation of constitutive transport vesicles involves the association of non-clathrin coat proteins to transport organelles
1,2
. Here we report that IgE receptors and protein kinase C (PKC) regulate the GTP-dependent binding of the two coat proteins ADP-ribosylation factor (ARF) and
β
-COP
3–5
to Golgi membranes in rat basophilic leukaemia cells. Activation of IgE receptors and PKC prevented the ARF and
β
-COP dissociation from Golgi membranes that occurs in permeabilized cells in the absence of GTP and potentiated the association-promoting effects of GTP and the G protein activator fluoroluminate. In contrast, PKC downregulation and PKC inhibition abolished the activity of GTP and fluoroluminate in promoting ARF binding to the Golgi complex. Studies of ARF binding to isolated Golgi membranes gave similar results. These findings suggest that coat assembly on Golgi membranes, and thus possibly constitutive secretory traffic, is modulated by membrane receptors and second messengers. |
| doi_str_mv | 10.1038/364818a0 |
| format | Article |
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1,2
. Here we report that IgE receptors and protein kinase C (PKC) regulate the GTP-dependent binding of the two coat proteins ADP-ribosylation factor (ARF) and
β
-COP
3–5
to Golgi membranes in rat basophilic leukaemia cells. Activation of IgE receptors and PKC prevented the ARF and
β
-COP dissociation from Golgi membranes that occurs in permeabilized cells in the absence of GTP and potentiated the association-promoting effects of GTP and the G protein activator fluoroluminate. In contrast, PKC downregulation and PKC inhibition abolished the activity of GTP and fluoroluminate in promoting ARF binding to the Golgi complex. Studies of ARF binding to isolated Golgi membranes gave similar results. These findings suggest that coat assembly on Golgi membranes, and thus possibly constitutive secretory traffic, is modulated by membrane receptors and second messengers.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/364818a0</identifier><identifier>PMID: 7689177</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Adenosine diphosphate ; ADP-Ribosylation Factors ; Aluminum - pharmacology ; Animals ; Brefeldin A ; Cell Membrane Permeability ; Coatomer Protein ; Cyclopentanes - pharmacology ; Enzyme Activation ; Fluorine - pharmacology ; Glycosaminoglycans - metabolism ; Golgi Apparatus - metabolism ; GTP-Binding Proteins - metabolism ; Guanosine 5'-O-(3-Thiotriphosphate) - pharmacology ; Guanosine Triphosphate - metabolism ; Humanities and Social Sciences ; letter ; Leukemia ; Medical research ; Membranes ; Microtubule-Associated Proteins - metabolism ; multidisciplinary ; Naphthalenes ; Phorbol Esters - pharmacology ; Polycyclic Compounds - pharmacology ; Protein Binding ; Protein Kinase C - antagonists & inhibitors ; Protein Kinase C - metabolism ; Proteins ; Rats ; Receptors, IgE - metabolism ; Rodents ; Science ; Science (multidisciplinary) ; Second Messenger Systems ; Tetradecanoylphorbol Acetate - pharmacology ; Tumor Cells, Cultured</subject><ispartof>Nature (London), 1993-08, Vol.364 (6440), p.818-821</ispartof><rights>Springer Nature Limited 1993</rights><rights>Copyright Macmillan Journals Ltd. Aug 26, 1993</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/364818a0$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/364818a0$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7689177$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>De Matteis, Maria Antonietta</creatorcontrib><creatorcontrib>Santini, Giovanna</creatorcontrib><creatorcontrib>Kahn, Richard A.</creatorcontrib><creatorcontrib>Di Tullio, Giuseppe</creatorcontrib><creatorcontrib>Luini, Alberto</creatorcontrib><title>Receptor and protein kinase C-mediated regulation of ARF binding to the Golgi complex</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>THE formation of constitutive transport vesicles involves the association of non-clathrin coat proteins to transport organelles
1,2
. Here we report that IgE receptors and protein kinase C (PKC) regulate the GTP-dependent binding of the two coat proteins ADP-ribosylation factor (ARF) and
β
-COP
3–5
to Golgi membranes in rat basophilic leukaemia cells. Activation of IgE receptors and PKC prevented the ARF and
β
-COP dissociation from Golgi membranes that occurs in permeabilized cells in the absence of GTP and potentiated the association-promoting effects of GTP and the G protein activator fluoroluminate. In contrast, PKC downregulation and PKC inhibition abolished the activity of GTP and fluoroluminate in promoting ARF binding to the Golgi complex. Studies of ARF binding to isolated Golgi membranes gave similar results. These findings suggest that coat assembly on Golgi membranes, and thus possibly constitutive secretory traffic, is modulated by membrane receptors and second messengers.</description><subject>Adenosine diphosphate</subject><subject>ADP-Ribosylation Factors</subject><subject>Aluminum - pharmacology</subject><subject>Animals</subject><subject>Brefeldin A</subject><subject>Cell Membrane Permeability</subject><subject>Coatomer Protein</subject><subject>Cyclopentanes - pharmacology</subject><subject>Enzyme Activation</subject><subject>Fluorine - pharmacology</subject><subject>Glycosaminoglycans - metabolism</subject><subject>Golgi Apparatus - metabolism</subject><subject>GTP-Binding Proteins - metabolism</subject><subject>Guanosine 5'-O-(3-Thiotriphosphate) - pharmacology</subject><subject>Guanosine Triphosphate - metabolism</subject><subject>Humanities and Social Sciences</subject><subject>letter</subject><subject>Leukemia</subject><subject>Medical research</subject><subject>Membranes</subject><subject>Microtubule-Associated Proteins - metabolism</subject><subject>multidisciplinary</subject><subject>Naphthalenes</subject><subject>Phorbol Esters - pharmacology</subject><subject>Polycyclic Compounds - pharmacology</subject><subject>Protein Binding</subject><subject>Protein Kinase C - antagonists & inhibitors</subject><subject>Protein Kinase C - metabolism</subject><subject>Proteins</subject><subject>Rats</subject><subject>Receptors, IgE - metabolism</subject><subject>Rodents</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Second Messenger Systems</subject><subject>Tetradecanoylphorbol Acetate - pharmacology</subject><subject>Tumor Cells, Cultured</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpdkV9LwzAUxYMoc07BLyAEHwQfqjdNmj-PY7gpDIThnkubpjWzS2rTgn57I04Eny7c8-Nw7j0IXRK4I0DlPeVMElnAEZoSJnjCuBTHaAqQygQk5afoLIQdAGREsAmaCC4VEWKKthujTTf4Hheuwl3vB2MdfrOuCAYvkr2pbDGYCvemGdtisN5hX-P5ZolL6yrrGjx4PLwavPJtY7H2-641H-fopC7aYC4Oc4a2y4eXxWOyfl49LebrpEspDElFdZ1lVNW0qrVUlTA1aEa0oRmtQAqeRkLVWnEBZaYFKM1rlYpSkLiilM7QzY9vDP4-mjDkexu0advCGT-GnHBOaMpVBK__gTs_9i5my1NgjANXLEJXB2gs4-F519t90X_mh2dF_fZHD1Fxjen_TAjk3z3kvz3QL9ccdjM</recordid><startdate>19930826</startdate><enddate>19930826</enddate><creator>De Matteis, Maria Antonietta</creator><creator>Santini, Giovanna</creator><creator>Kahn, Richard A.</creator><creator>Di Tullio, Giuseppe</creator><creator>Luini, Alberto</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7ST</scope><scope>7T5</scope><scope>7TG</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88G</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2M</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PSYQQ</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>R05</scope><scope>RC3</scope><scope>S0X</scope><scope>SOI</scope></search><sort><creationdate>19930826</creationdate><title>Receptor and protein kinase C-mediated regulation of ARF binding to the Golgi complex</title><author>De Matteis, Maria Antonietta ; Santini, Giovanna ; Kahn, Richard A. ; Di Tullio, Giuseppe ; Luini, Alberto</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p230t-d3cf5539f3dfc89d7ef0c41ce353d08762d3c9fc9670b5c709c6f927b71967333</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Adenosine diphosphate</topic><topic>ADP-Ribosylation Factors</topic><topic>Aluminum - 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1,2
. Here we report that IgE receptors and protein kinase C (PKC) regulate the GTP-dependent binding of the two coat proteins ADP-ribosylation factor (ARF) and
β
-COP
3–5
to Golgi membranes in rat basophilic leukaemia cells. Activation of IgE receptors and PKC prevented the ARF and
β
-COP dissociation from Golgi membranes that occurs in permeabilized cells in the absence of GTP and potentiated the association-promoting effects of GTP and the G protein activator fluoroluminate. In contrast, PKC downregulation and PKC inhibition abolished the activity of GTP and fluoroluminate in promoting ARF binding to the Golgi complex. Studies of ARF binding to isolated Golgi membranes gave similar results. These findings suggest that coat assembly on Golgi membranes, and thus possibly constitutive secretory traffic, is modulated by membrane receptors and second messengers.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>7689177</pmid><doi>10.1038/364818a0</doi><tpages>4</tpages></addata></record> |
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| ispartof | Nature (London), 1993-08, Vol.364 (6440), p.818-821 |
| issn | 0028-0836 1476-4687 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_16613269 |
| source | MEDLINE; SpringerLink Journals; Nature Journals Online |
| subjects | Adenosine diphosphate ADP-Ribosylation Factors Aluminum - pharmacology Animals Brefeldin A Cell Membrane Permeability Coatomer Protein Cyclopentanes - pharmacology Enzyme Activation Fluorine - pharmacology Glycosaminoglycans - metabolism Golgi Apparatus - metabolism GTP-Binding Proteins - metabolism Guanosine 5'-O-(3-Thiotriphosphate) - pharmacology Guanosine Triphosphate - metabolism Humanities and Social Sciences letter Leukemia Medical research Membranes Microtubule-Associated Proteins - metabolism multidisciplinary Naphthalenes Phorbol Esters - pharmacology Polycyclic Compounds - pharmacology Protein Binding Protein Kinase C - antagonists & inhibitors Protein Kinase C - metabolism Proteins Rats Receptors, IgE - metabolism Rodents Science Science (multidisciplinary) Second Messenger Systems Tetradecanoylphorbol Acetate - pharmacology Tumor Cells, Cultured |
| title | Receptor and protein kinase C-mediated regulation of ARF binding to the Golgi complex |
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