Regulation of G-protein activation by mastoparans and other cationic peptides

E. M. Ross, T. Higashijima

Research output: Contribution to journalArticlepeer-review

21 Scopus citations


This chapter discusses regulation of G-protein activation by mastoparans and other cationic properties. Mastoparan, Ile-Asn-Leu-Lys-Ala-Leu-Ala-Ala-Leu-Ala-Lys-Lys-Ile- Leu-amide (MP), activates G proteins by catalyzing Guanosine-5'-triphosphate (GTP)/Leu-amide (MP), by catalyzing GTP/GDP exchange, the mechanism of action of G-protein-coupled receptors. Like receptors, MP accelerates guanine nucleotide exchange at micromolar Mg2+, it does not alter hydrolysis of bound GTP, its action is markedly potentiated by G-protein fly subunits, and it is blocked by pertussis toxin-catalyzed ADP-ribosylation of the target α subunit. The MPs are prototypical of a wide variety of amphiphilic, cationic peptides that activates G proteins. MP is a natural component of wasp venom, and at least seven MP analogs are produced by different species. Regulatory activity requires that a G-protein-stimulating peptide be both amphiphilic and cationic. Helix-breaking residues or charged residues on what should be the hydrophobic face of the helix both diminish activity dramatically. Mas17, with a lysyl residue on the hydrophobic side of the helix, is a commercially available negative control for experiments where MP is used to alter G-protein activation.

Original languageEnglish (US)
Pages (from-to)26-37
Number of pages12
JournalMethods in Enzymology
Issue numberC
StatePublished - Jan 1 1994

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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