Identification of rho as a substrate for botulinum toxin C3‐catalyzed ADP‐ribosylation

FEBS Letters

Quilliam, Lawrence A.¹  Bokoch, Gary M.¹  Lacal, Juan-Carlos² 

[1] Department of Immunology, Research Institute of Scripps Clinic, La Jolla, CA 92037, USA;Laboratory of Cellular and Molecular Biology, National Cancer Institute, Bethesda, MD 20892, USA

关键词: GTP-binding protein;    Gene;    ras;    Protein;    Rho;    Botulinum toxin;    ATP-ribosylation;   

DOI  :  10.1016/0014-5793(89)81339-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Recombinant Aplysia rho and a GTP-binding protein purified from human neutrophil membranes (G_22K) were ADP-ribosylated by botulinum toxin C₃ with stoichiometries of 0.8 and 0.6, respectively. Rho and G_22K appeared to be different proteins since (i) rho migrated faster on polyacrylamide gels, (ii) unlike G_22K, rho did not require the presence of cytosol to be ADP-ribosylated, (iii) G_22K was not recognized by an anti-rho antiserum, and (iv) antibody 142-24E05 recognized G_22K effectively but only poorly cross reacted with rho. ADP-ribosylation had no effect on the ability of rho to bind or hydrolyse GTP. Therefore, it appears that there are multiple botulinum toxin C₃ substrates and that the toxin exerts its effects on cell function by a mechanism other than modulating the GTPase activity of rho.

【 授权许可】

Unknown