Pasteurella multocida toxin facilitates inositol phosphate formation by bombesin through tyrosine phosphorylation of Gαq

被引：16

作者：

Baldwin, MR ^{[1
]}

Pullinger, GD ^{[1
]}

Lax, AJ ^{[1
]}

机构：

[1] Guys Hosp, Univ London Kings Coll, Inst Dent, Dept Microbiol, London SE1 9RT, England

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2003年 / 278卷 / 35期

关键词：

D O I：

10.1074/jbc.M303524200

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The intracellularly acting Pasteurella multocida toxin (PMT) is a potent mitogen that stimulates G(q)-dependent formation of inositol trisphosphate. We show that PMT, a nontoxic mutant of PMT (PMTC1165S), and bombesin each stimulate time-dependent phosphorylation of Galpha(q) at tyrosine 349. Although PMT and PMTC1165S each cause phosphorylation of Galpha(q), only the wild-type toxin activates G(q). Pretreatment of cells with wild-type or mutant PMT potentiated the formation of inositol phosphates stimulated by bombesin equally. These data show that PMT potentiates bombesin receptor signaling through tyrosine phosphorylation of G(q) and distinguishes between the two proposed models of G(q) activation, showing that tyrosine phosphorylation is not linked to receptor uncoupling.

引用

页码：32719 / 32725

页数：7

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