Stimulation of endogenous ADP-ribosylation by brefeldin A
Brefeldin A (BFA) is a fungal metabolite that exerts profound and generally inhibitory actions on membrane transport. At least some of the BFA effects are due to inhibition of the GDP-GTP exchange on the ADP-ribosylation factor (ARF) catalyzed by membrane protein(s). ARF activation is likely to be a...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1994-02, Vol.91 (3), p.1114-1118 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | De Matteis, M A Di Girolamo, M Colanzi, A Pallas, M Di Tullio, G McDonald, L J Moss, J Santini, G Bannykh, S Corda, D |
| description | Brefeldin A (BFA) is a fungal metabolite that exerts profound and generally inhibitory actions on membrane transport. At least some of the BFA effects are due to inhibition of the GDP-GTP exchange on the ADP-ribosylation factor (ARF) catalyzed by membrane protein(s). ARF activation is likely to be a key event in the association of non-clathrin coat components, including ARF itself, onto transport organelles. ARF, in addition to participating in membrane transport, is known to function as a cofactor in the enzymatic activity of cholera toxin, a bacterial ADP-ribosyltransferase. In this study we have examined whether BFA, in addition to inhibiting membrane transport, might affect endogenous ADP-ribosylation in eukaryotic cells. Two cytosolic proteins of 38 and 50 kDa were enzymatically ADP-ribosylated in the presence of BFA in cellular extracts. The 38-kDa substrate was tentatively identified as the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase. The BFA-binding components mediating inhibition of membrane traffic and stimulation of ADP-ribosylation appear to have the same ligand specificity. These data demonstrate the existence of a BFA-sensitive mono(ADP-ribosyl)transferase that may play a role in membrane movements. |
| doi_str_mv | 10.1073/pnas.91.3.1114 |
| format | Article |
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At least some of the BFA effects are due to inhibition of the GDP-GTP exchange on the ADP-ribosylation factor (ARF) catalyzed by membrane protein(s). ARF activation is likely to be a key event in the association of non-clathrin coat components, including ARF itself, onto transport organelles. ARF, in addition to participating in membrane transport, is known to function as a cofactor in the enzymatic activity of cholera toxin, a bacterial ADP-ribosyltransferase. In this study we have examined whether BFA, in addition to inhibiting membrane transport, might affect endogenous ADP-ribosylation in eukaryotic cells. Two cytosolic proteins of 38 and 50 kDa were enzymatically ADP-ribosylated in the presence of BFA in cellular extracts. The 38-kDa substrate was tentatively identified as the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase. The BFA-binding components mediating inhibition of membrane traffic and stimulation of ADP-ribosylation appear to have the same ligand specificity. These data demonstrate the existence of a BFA-sensitive mono(ADP-ribosyl)transferase that may play a role in membrane movements.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.91.3.1114</identifier><identifier>PMID: 8302839</identifier><language>eng</language><publisher>United States: National Acad Sciences</publisher><subject>Adenosine Diphosphate Ribose - metabolism ; ADP Ribose Transferases ; ADP-Ribosylation Factors ; Animals ; Biological Transport, Active ; Brefeldin A ; Cell Line ; Cellular biology ; Cyclopentanes - pharmacology ; Fungi ; Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism ; GTP-Binding Proteins - metabolism ; Membranes ; Mycotoxins - pharmacology ; NAD - metabolism ; Poly(ADP-ribose) Polymerases - metabolism ; Proteins - metabolism ; Rats ; Substrate Specificity</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1994-02, Vol.91 (3), p.1114-1118</ispartof><rights>Copyright National Academy of Sciences Feb 1, 1994</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c561t-616e59e839dd7ece79272348bf79ae0fae7abb502d1e3128d7a96744393ea5613</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/91/3.cover.gif</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC521464/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC521464/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8302839$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>De Matteis, M A</creatorcontrib><creatorcontrib>Di Girolamo, M</creatorcontrib><creatorcontrib>Colanzi, A</creatorcontrib><creatorcontrib>Pallas, M</creatorcontrib><creatorcontrib>Di Tullio, G</creatorcontrib><creatorcontrib>McDonald, L J</creatorcontrib><creatorcontrib>Moss, J</creatorcontrib><creatorcontrib>Santini, G</creatorcontrib><creatorcontrib>Bannykh, S</creatorcontrib><creatorcontrib>Corda, D</creatorcontrib><title>Stimulation of endogenous ADP-ribosylation by brefeldin A</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Brefeldin A (BFA) is a fungal metabolite that exerts profound and generally inhibitory actions on membrane transport. At least some of the BFA effects are due to inhibition of the GDP-GTP exchange on the ADP-ribosylation factor (ARF) catalyzed by membrane protein(s). ARF activation is likely to be a key event in the association of non-clathrin coat components, including ARF itself, onto transport organelles. ARF, in addition to participating in membrane transport, is known to function as a cofactor in the enzymatic activity of cholera toxin, a bacterial ADP-ribosyltransferase. In this study we have examined whether BFA, in addition to inhibiting membrane transport, might affect endogenous ADP-ribosylation in eukaryotic cells. Two cytosolic proteins of 38 and 50 kDa were enzymatically ADP-ribosylated in the presence of BFA in cellular extracts. The 38-kDa substrate was tentatively identified as the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase. The BFA-binding components mediating inhibition of membrane traffic and stimulation of ADP-ribosylation appear to have the same ligand specificity. These data demonstrate the existence of a BFA-sensitive mono(ADP-ribosyl)transferase that may play a role in membrane movements.</description><subject>Adenosine Diphosphate Ribose - metabolism</subject><subject>ADP Ribose Transferases</subject><subject>ADP-Ribosylation Factors</subject><subject>Animals</subject><subject>Biological Transport, Active</subject><subject>Brefeldin A</subject><subject>Cell Line</subject><subject>Cellular biology</subject><subject>Cyclopentanes - pharmacology</subject><subject>Fungi</subject><subject>Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism</subject><subject>GTP-Binding Proteins - metabolism</subject><subject>Membranes</subject><subject>Mycotoxins - pharmacology</subject><subject>NAD - metabolism</subject><subject>Poly(ADP-ribose) Polymerases - metabolism</subject><subject>Proteins - metabolism</subject><subject>Rats</subject><subject>Substrate Specificity</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkb1PwzAQxS0EgvKxsiFFDGwJPtuJ44Gh4ltCAgmYLSe5lKDULnGC6H-Pq5aqICYP7_fO7-4Rcgw0ASr5-cwanyhIeAIAYouMgCqIM6HoNhlRymScCyb2yL7375RSleZ0l-zmnLKcqxFRz30zHVrTN85Gro7QVm6C1g0-Gl89xV1TOD9fycU8Kjqssa0aG40PyU5tWo9Hq_eAvN5cv1zexQ-Pt_eX44e4TDPo4wwyTBWGz6pKYolSMcm4yItaKoO0NihNUaSUVYAcWF5JozIpBFccTZjAD8jFcu5sKKZYlWj7zrR61jVT0821M43-rdjmTU_cp04ZiEwE_9nK37mPAX2vp40vsW2NxbCmhkxmXCkZwNM_4LsbOht204wCZyGSClCyhMrOeR-usQ4CVC8K0YtCtALN9aKQYDjZjL_GVw1sxFv4ftS1X9dD2_b41W8M-hfk321VniM</recordid><startdate>19940201</startdate><enddate>19940201</enddate><creator>De Matteis, M A</creator><creator>Di Girolamo, M</creator><creator>Colanzi, A</creator><creator>Pallas, M</creator><creator>Di Tullio, G</creator><creator>McDonald, L J</creator><creator>Moss, J</creator><creator>Santini, G</creator><creator>Bannykh, S</creator><creator>Corda, D</creator><general>National Acad Sciences</general><general>National Academy of Sciences</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7U7</scope><scope>5PM</scope></search><sort><creationdate>19940201</creationdate><title>Stimulation of endogenous ADP-ribosylation by brefeldin A</title><author>De Matteis, M A ; 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| subjects | Adenosine Diphosphate Ribose - metabolism ADP Ribose Transferases ADP-Ribosylation Factors Animals Biological Transport, Active Brefeldin A Cell Line Cellular biology Cyclopentanes - pharmacology Fungi Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism GTP-Binding Proteins - metabolism Membranes Mycotoxins - pharmacology NAD - metabolism Poly(ADP-ribose) Polymerases - metabolism Proteins - metabolism Rats Substrate Specificity |
| title | Stimulation of endogenous ADP-ribosylation by brefeldin A |
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