TY - JOUR
T1 - Regulation of G-protein activation by mastoparans and other cationic peptides
AU - Ross, E. M.
AU - Higashijima, T.
N1 - Copyright:
Copyright 2018 Elsevier B.V., All rights reserved.
PY - 1994/1/1
Y1 - 1994/1/1
N2 - 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.
AB - 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.
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U2 - 10.1016/S0076-6879(94)37050-8
DO - 10.1016/S0076-6879(94)37050-8
M3 - Article
C2 - 7935002
AN - SCOPUS:0028037835
SN - 0076-6879
VL - 237
SP - 26
EP - 37
JO - Methods in Enzymology
JF - Methods in Enzymology
IS - C
ER -