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  • 1
    Online Resource
    Online Resource
    Inverse control of Rab proteins by Yersinia ADP-ribosyltransferase and glycosyltransferase related to clostridial glucosylating toxins
    American Association for the Advancement of Science (AAAS) ; 2020
    In:  Science Advances Vol. 6, No. 11 ( 2020-03-13)
    Details
    In: Science Advances, American Association for the Advancement of Science (AAAS), Vol. 6, No. 11 ( 2020-03-13)
    Abstract: We identified a glucosyltransferase (YGT) and an ADP-ribosyltransferase (YART) in Yersinia mollaretii , highly related to glucosylating toxins from Clostridium difficile , the cause of antibiotics-associated enterocolitis. Both Yersinia toxins consist of an amino-terminal enzyme domain, an autoprotease domain activated by inositol hexakisphosphate, and a carboxyl-terminal translocation domain. YGT N -acetylglucosaminylates Rab5 and Rab31 at Thr 52 and Thr 36 , respectively, thereby inactivating the Rab proteins. YART ADP-ribosylates Rab5 and Rab31 at Gln 79 and Gln 64 , respectively. This activates Rab proteins by inhibiting GTP hydrolysis. We determined the crystal structure of the glycosyltransferase domain of YGT (YGT G ) in the presence and absence of UDP at 1.9- and 3.4-Å resolution, respectively. Thereby, we identified a previously unknown potassium ion–binding site, which explains potassium ion–dependent enhanced glycosyltransferase activity in clostridial and related toxins. Our findings exhibit a novel type of inverse regulation of Rab proteins by toxins and provide new insights into the structure-function relationship of glycosyltransferase toxins.
    Type of Medium: Online Resource
    ISSN: 2375-2548
    URL: Article
    DOI: 10.1126/sciadv.aaz2094
    Language: English
    Publisher: American Association for the Advancement of Science (AAAS)
    Publication Date: 2020
    detail.hit.zdb_id: 2810933-8
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  • 2
    Online Resource
    Online Resource
    Neuropeptide Y inhibits renin release by a pertussis toxin-sensitive mechanism
    American Physiological Society ; 1987
    In:  American Journal of Physiology-Renal Physiology Vol. 252, No. 3 ( 1987-03-01), p. F543-F550
    Details
    In: American Journal of Physiology-Renal Physiology, American Physiological Society, Vol. 252, No. 3 ( 1987-03-01), p. F543-F550
    Abstract: The effects of neuropeptide Y (NPY) were studied in the isolated rat kidney, which was perfused at constant perfusion pressure with a synthetic medium. In this preparation NPY produced concentration (1-100 nM)-dependent inhibition of renin release and vasoconstriction. In kidneys perfused at constant flow, inhibition of renin release by NPY was even more pronounced, excluding a flow-dependent washout effect. The simultaneous infusion of the calcium channel antagonist methoxyverapamil (2 microM) or of the calmodulin inhibitor calmidazolium (1 microM) did not prevent these effects of NPY, suggesting that calcium-dependent reactions are not primarily involved. Inhibition of renin release by NPY was also observed in tissue pieces prepared from the hydronephrotic rat kidney, in which tubular elements are lacking. This indicates that inhibition of renin release by NPY is not dependent on the presence of macula densa cells or on changes of intrarenal hemodynamics. In isolated kidneys from rats pretreated with pertussis toxin (2 micrograms/100 g ip) both effects of NPY, renal vasoconstriction and inhibition of renin release, were almost completely abolished. The pertussis toxin-sensitive factor mediating the effects of NPY is most likely the Ni-coupling protein of the adenylate cyclase complex. Accordingly, our data suggest that NPY induces renal vasoconstriction and inhibits renin release by inhibition of adenylate cyclase activity in vascular smooth muscle and renin-producing cells.
    Type of Medium: Online Resource
    ISSN: 1931-857X , 1522-1466
    URL: Article
    DOI: 10.1152/ajprenal.1987.252.3.F543
    Language: English
    Publisher: American Physiological Society
    Publication Date: 1987
    detail.hit.zdb_id: 1477287-5
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  • 3
    Online Resource
    Online Resource
    Role of host cell chaperones in cellular uptake of binary clostridial enterotoxins
    Elsevier BV ; 2016
    In:  Toxicon Vol. 116 ( 2016-06), p. 75-
    Details
    In: Toxicon, Elsevier BV, Vol. 116 ( 2016-06), p. 75-
    Type of Medium: Online Resource
    ISSN: 0041-0101
    URL: Article
    DOI: 10.1016/j.toxicon.2016.01.013
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2016
    detail.hit.zdb_id: 1498784-3
    SSG: 12
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  • 4
    Online Resource
    Online Resource
    RhoA exerts a permissive effect on volume-regulated anion channels in vascular endothelial cells
    American Physiological Society ; 2002
    In:  American Journal of Physiology-Cell Physiology Vol. 283, No. 1 ( 2002-07-01), p. C115-C125
    Details
    In: American Journal of Physiology-Cell Physiology, American Physiological Society, Vol. 283, No. 1 ( 2002-07-01), p. C115-C125
    Abstract: Cell swelling triggers in most cell types an outwardly rectifying anion current, I Cl,swell , via volume-regulated anion channels (VRACs). We have previously demonstrated in calf pulmonary artery endothelial (CPAE) cells that inhibition of the Rho/Rho kinase/myosin light chain phosphorylation pathway reduces the swelling-dependent activation of I Cl,swell . However, these experiments did not allow us to discriminate between a direct activator role or a permissive effect. We now show that the Rho pathway did not affect VRAC activity if this pathway was activated by transfecting CPAE cells with constitutively active isoforms of Gα (a Rho activating heterotrimeric G protein subunit), Rho, or Rho kinase. Furthermore, biochemical and morphological analysis failed to demonstrate activation of the Rho pathway during hypotonic cell swelling. Finally, manipulating the Rho pathway with either guanosine 5′- O-(3-thiotriphosphate) or C3 exoenzyme had no effect on VRACs in caveolin-1-expressing Caco-2 cells. We conclude that the Rho pathway exerts a permissive effect on VRACs in CPAE cells, i.e., swelling-induced opening of VRACs requires a functional Rho pathway, but not an activation of the Rho pathway.
    Type of Medium: Online Resource
    ISSN: 0363-6143 , 1522-1563
    URL: Article
    DOI: 10.1152/ajpcell.00038.2001
    Language: English
    Publisher: American Physiological Society
    Publication Date: 2002
    detail.hit.zdb_id: 1477334-X
    SSG: 12
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  • 5
    Online Resource
    Online Resource
    Botulinum C2 toxin treatment increases the G-actin pool in intact chicken cells: A model for the cytopathic action of actin-ADP-ribosylating toxins
    Elsevier BV ; 1989
    In:  Toxicon Vol. 27, No. 9 ( 1989-1), p. 989-993
    Details
    In: Toxicon, Elsevier BV, Vol. 27, No. 9 ( 1989-1), p. 989-993
    Type of Medium: Online Resource
    ISSN: 0041-0101
    URL: Article
    DOI: 10.1016/0041-0101(89)90149-9
    Language: English
    Publisher: Elsevier BV
    Publication Date: 1989
    detail.hit.zdb_id: 1498784-3
    SSG: 12
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  • 6
    Online Resource
    Online Resource
    Buchbesprechungen
    Springer Science and Business Media LLC ; 1985
    In:  Klinische Wochenschrift Vol. 63, No. 5 ( 1985-3), p. 238-240
    Details
    In: Klinische Wochenschrift, Springer Science and Business Media LLC, Vol. 63, No. 5 ( 1985-3), p. 238-240
    Type of Medium: Online Resource
    ISSN: 0023-2173 , 1432-1440
    URL: Article
    DOI: 10.1007/BF01731178
    RVK:
    XA 10000
    Language: German
    Publisher: Springer Science and Business Media LLC
    Publication Date: 1985
    detail.hit.zdb_id: 1462132-0
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  • 7
    Online Resource
    Online Resource
    Evidence for two GTPases activated by thrombin in membranes of human platelets
    Portland Press Ltd. ; 1986
    In:  Biochemical Journal Vol. 237, No. 3 ( 1986-08-01), p. 669-674
    Details
    In: Biochemical Journal, Portland Press Ltd., Vol. 237, No. 3 ( 1986-08-01), p. 669-674
    Abstract: Thrombin inhibits adenylate cyclase and stimulates GTP hydrolysis by high-affinity GTPase(s) in membranes of human platelets at almost identical concentrations. Both of these thrombin actions are similar to those observed with agonist-activated alpha 2-adrenoceptors coupling to the inhibitory guanine nucleotide-binding protein N1. However, stimulation of GTP hydrolysis caused by adrenaline (alpha 2-adrenoceptor agonist) and by thrombin at maximally effective concentrations was partially additive, whereas with regard to adenylate cyclase inhibition no additive response was observed. Furthermore, treatment of platelet membranes with pertussis toxin, which inactivates Ni and largely abolishes thrombin- and adrenaline-induced adenylate cyclase inhibition and adrenaline-induced GTPase stimulation, decreased the thrombin-induced stimulation of GTP hydrolysis by only about 30%. Additionally, the thiol reagent N-ethylmalemide (NEM) at rather low concentrations abolished thrombin- and adrenaline-induced stimulation of GTP hydrolysis was decreased by only 30-40% by treatment of platelet membranes with even high concentrations of NEM. Treatment with cholera toxin, which inhibits GTPase activity of the Ns (stimulatory guanine nucleotide-binding) protein, has no effect on thrombin-stimulated GTP hydrolysis. The data suggest that thrombin interaction with its receptor sites in platelet membranes leads to stimulation of two GTP-hydrolysing enzymes. One of these enzymes is apparently Ni and is also activated by agonist-activated alpha 2-adrenoceptors and is inactivated by pertussis toxin and NEM treatment. The other GTP-hydrolysing enzyme activated by thrombin may represent a guanine nucleotide-binding protein apparently involved in the coupling of thrombin receptors to the phosphoinositide phosphodiesterase.
    Type of Medium: Online Resource
    ISSN: 0264-6021 , 1470-8728
    URL: Article
    DOI: 10.1042/bj2370669
    RVK:
    WA 15000
    Language: English
    Publisher: Portland Press Ltd.
    Publication Date: 1986
    detail.hit.zdb_id: 1473095-9
    SSG: 12
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  • 8
    Online Resource
    Online Resource
    Stimulation of high-affinity GTPase by trypsin and trypsin-like proteinases in membranes of human platelets
    Portland Press Ltd. ; 1988
    In:  Biochemical Journal Vol. 249, No. 3 ( 1988-02-01), p. 639-643
    Details
    In: Biochemical Journal, Portland Press Ltd., Vol. 249, No. 3 ( 1988-02-01), p. 639-643
    Abstract: The influence of various proteinases on GTP hydrolysis was studied in membranes of human platelets. Of the proteinases examined, trypsin, acrosin and a recently described trypsin-like proteinase from bovine sperm, but not chymotrypsin, increased GTP hydrolysis. Similar to what was described previously for hormone-like agents, the stimulation of GTP hydrolysis by the proteinases was only observed at low GTP concentrations, with apparent Km values of 0.2-0.3 microM-GTP. Stimulation of the high-affinity GTPase by the proteinases occurred without apparent lag phase and was constant over a long period of incubation. The proteinase inhibitors leupeptin and soya-bean trypsin inhibitor blocked the stimulation of GTP hydrolysis, but did not reverse the effect of the proteinases. Treatment of platelet membranes with N-ethylmaleimide, which eliminates Gi-protein (inhibitory guanine-nucleotide-binding protein)-related GTPase stimulation by adrenaline, decreased stimulation of GTP hydrolysis by the proteinases only partially. Activation of GTP hydrolysis by the proteinases was partially additive with that caused by adrenaline, whereas thrombin stimulation was not increased further. The data indicate that, similarly to the proteinase thrombin, trypsin and trypsin-like proteinases can activate GTP-hydrolysing protein(s) that exhibit high affinity for GTP in platelet membranes. It is suggested that the proteinases interact in platelet membranes with a receptor site similar to that used by thrombin and that the observed GTPase stimulation is a reflection of a proteinase-receptor interaction with a guanine-nucleotide-binding regulatory protein.
    Type of Medium: Online Resource
    ISSN: 0264-6021 , 1470-8728
    URL: Article
    DOI: 10.1042/bj2490639
    RVK:
    WA 15000
    Language: English
    Publisher: Portland Press Ltd.
    Publication Date: 1988
    detail.hit.zdb_id: 1473095-9
    SSG: 12
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  • 9
    Online Resource
    Online Resource
    Botulinum C2 toxin ADP-ribosylates actin
    Springer Science and Business Media LLC ; 1986
    In:  Nature Vol. 322, No. 6077 ( 1986-7), p. 390-392
    Details
    In: Nature, Springer Science and Business Media LLC, Vol. 322, No. 6077 ( 1986-7), p. 390-392
    Type of Medium: Online Resource
    ISSN: 0028-0836 , 1476-4687
    URL: Article
    DOI: 10.1038/322390a0
    RVK:
    TA 1000
    RVK:
    UA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 1986
    detail.hit.zdb_id: 120714-3
    detail.hit.zdb_id: 1413423-8
    SSG: 11
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  • 10
    Online Resource
    Online Resource
    Acceleration of the adipocyte adenylate cyclase turn-off reaction by inhibitory hormonal factors.
    Proceedings of the National Academy of Sciences ; 1982
    In:  Proceedings of the National Academy of Sciences Vol. 79, No. 5 ( 1982-03), p. 1373-1377
    Details
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 79, No. 5 ( 1982-03), p. 1373-1377
    Abstract: beta-Adrenergic agonists such as isoproterenol stimulate hamster adipocyte adenylate cyclase by a GTP-dependent process, whereas prostaglandin E1, alpha-adrenergic agonists, and nicotinic acid inhibit the enzyme by a process also dependent on GTP and amplified by sodium ions. We have determined the first-order rate constant describing the decay of isoproterenol plus GTP-stimulated adenylate cyclase and the modulation of this off rate constant by sodium and inhibitory hormonal factors. With 1 microM GTP and 0.2 mM isoproterenol, the off rate constant was 5.0 min-1 at 25 degrees C. Addition of NaCl (100 mM), which increased basal and isoproterenol-stimulated cyclase activities, decreased the rate constant of the hormone-stimulated enzyme to 1.4 min-1. Prostaglandin E1 (10 microM) and nicotinic acid (30 microM), which decreased basal and hormonally stimulated enzyme activities, increased the NaCl-suppressed off rate constant to 6.1 and 6.0 min-1, respectively. Similar data were obtained with 1 mM isoproterenol with MnATP and MgATP as the adenylate cyclase substrate. On the other hand, the turn-on reaction of adipocyte adenylate cyclase, measured with the stable GTP analogue 5'-guanylyl imidodiphosphate (30 microM), was accelerated by isoproterenol (1 mM) and NaCl (100 mM). Under all of these conditions, inhibitory hormonal agents did not cause any delay in the turn-on reaction. These data indicate that, in hamster adipocyte membranes, inhibitory hormonal factors inhibit adenylate cyclase by increasing the enzyme's turn-off reaction.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    URL: Article
    DOI: 10.1073/pnas.79.5.1373
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 1982
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
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