The mammalian G protein rhoC is ADP-ribosylated by Clostridium botulinum exoenzyme C3 and affects actin microfilaments in Vero cells

EMBO J. 1989 Apr;8(4):1087-92.

Abstract

Clostridium botulinum C3 is a recently discovered exoenzyme that ADP-ribosylates a eukaryotic GTP-binding protein of the ras superfamily. We show now that the bacterially-expressed product of the human rhoC gene is ADP-ribosylated by C3 and corresponds in size, charge and behavior to the dominant C3 substrate of eukaryotic cells. C3 treatment of Vero cells results in the disappearance of microfilaments and in actinomorphic shape changes without any apparent direct effect upon actin. Thus the ADP-ribosylation of a rho protein seems to be responsible for microfilament disassembly and we infer that the unmodified form of a rho protein may be involved in cytoskeletal control.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • ADP Ribose Transferases / metabolism*
  • Actin Cytoskeleton / drug effects
  • Actin Cytoskeleton / metabolism
  • Actins / metabolism*
  • Adenosine Diphosphate Ribose / metabolism*
  • Animals
  • Botulinum Toxins*
  • Clostridium botulinum / enzymology
  • GTP-Binding Proteins / metabolism*
  • GTP-Binding Proteins / pharmacology
  • Humans
  • Magnesium / metabolism
  • Membrane Proteins / metabolism*
  • Membrane Proteins / pharmacology
  • Vero Cells
  • rho GTP-Binding Proteins*
  • rhoC GTP-Binding Protein

Substances

  • Actins
  • Membrane Proteins
  • Adenosine Diphosphate Ribose
  • ADP Ribose Transferases
  • exoenzyme C3, Clostridium botulinum
  • Botulinum Toxins
  • GTP-Binding Proteins
  • RHOC protein, human
  • rho GTP-Binding Proteins
  • rhoC GTP-Binding Protein
  • Magnesium