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

Lawrence Quilliam, Juan Carlos Lacal, Gary M. Bokoch

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

Recombinant Aplysia rho and a GTP-binding protein purified from human neutrophil membranes (G22K) were ADP-ribosylated by botulinum toxin C3 with stoichiometries of 0.8 and 0.6, respectively. Rho and G22K appeared to be different proteins since (i) rho migrated faster on polyacrylamide gels, (ii) unlike G22K, rho did not require the presence of cytosol to be ADP-ribosylated, (iii) G22K was not recognized by an anti-rho antiserum, and (iv) antibody 142-24E05 recognized G22K 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.

Original languageEnglish (US)
Pages (from-to)221-226
Number of pages6
JournalFEBS Letters
Volume247
Issue number2
DOIs
StatePublished - Apr 24 1989
Externally publishedYes

Fingerprint

Botulinum Toxins
Adenosine Diphosphate
rho GTP-Binding Proteins
Substrates
Aplysia
GTP Phosphohydrolases
Guanosine Triphosphate
GTP-Binding Proteins
Stoichiometry
Cytosol
Immune Sera
Neutrophils
Membranes
Antibodies
Proteins

Keywords

  • ATP-ribosylation
  • Botulinum toxin
  • Gene, ras
  • GTP-binding protein
  • Protein, Rho

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Identification of rho as a substrate for botulinum toxin C3-catalyzed ADP-ribosylation. / Quilliam, Lawrence; Lacal, Juan Carlos; Bokoch, Gary M.

In: FEBS Letters, Vol. 247, No. 2, 24.04.1989, p. 221-226.

Research output: Contribution to journalArticle

Quilliam, Lawrence ; Lacal, Juan Carlos ; Bokoch, Gary M. / Identification of rho as a substrate for botulinum toxin C3-catalyzed ADP-ribosylation. In: FEBS Letters. 1989 ; Vol. 247, No. 2. pp. 221-226.
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