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ADP-ribosylation of rho/rac gene products by botulinum ADP-ribosyltransferase C3;Application for study of small molecular GTP-binding protein functions. Narito MORII 1 , Shuh NARUMIYA 1 1Department of Pharmacology, Kyoto University Faculty of Medicine pp.539-549
Published Date 1991/8/10
DOI https://doi.org/10.11477/mf.1431900155
  • Abstract
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Clostridium botulinum types C and D produces a novel 25 kda ADP-ribosyltransferase, named botulinum ADP-ribosyltransferase C3, which modifies a group of 20-25 kda cellular proteins. At present three rho (rho A, B and C) and two rac (rac 1 and 2) gene products are identified as ADP-ribosylation substrates for C3 enzyme. They are low molecular weight GTP-hinding proteins sharing about 40% homology with ras p21s. The ADP-ribosylation occurs at asparagine residue located in their putative effector domain. This modification dose not change their GTP-binding or GTPase activities. Neither dose it affect the interaction of rho protein with the purified rho-specific GTPase activating protein. However, the addition of C3 enzyme to cultured PC-12 cells causes the in situ ADP-ribosylation of the rho/rac proteins and induces differentiated phenotypic changes in the cells. These results suggest that ADP-ribosylation of rho/rac proteins interferes their interaction with yet unidentified effector molecules downstream in the signal transduction pathway. Detailed mechanism of this effect of ADP-ribosylation and functions of the rho/rac proteins in the cells are currently under analysis.


Copyright © 1991, Igaku-Shoin Ltd. All rights reserved.

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電子版ISSN 1882-1243 印刷版ISSN 0001-8724 医学書院

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