Wasp venom toxin mastoparan, a histamine releaser from mast cells, is a direct activator of GTP-binding regulatory proteins

Higashijima, Tsutomu; Uzu, Sonoko; Nakajima, Terumi; Miyazawa, Tatsuo

doi:10.1007/978-94-010-9595-2_93

Cited by 22 publications

(31 citation statements)

References 15 publications

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“…These peptides probably resemble cthelical cytosolic domains of G protein-coupled receptors (see above) [22]. Consequently, peptides derived from receptor domains suggested to couple to G proteins are also used.…”

Section: All Rights Reservedmentioning

confidence: 99%

Potential roles of heterotrimeric G proteins of the endomembrane system

Nürnberg

Ahnert‐Hilger

1996

FEBS Letters

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Section: All Rights Reservedmentioning

confidence: 99%

Potential roles of heterotrimeric G proteins of the endomembrane system

Nürnberg

Ahnert‐Hilger

1996

FEBS Letters

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“…G proteins were alkylated with N-ethylmaleimide (NEM) prior to electrophoresis as in [14]. Immunoblot analysis was performed as in [ 11,15,16]. Antibodies used in the present experiments were anti-OLo (A) which was affinity-purified rabbit polyclonal IgG raised against purified O~o and anti-c~o (B) which was also affinity-purified rabbit polyclonal antibody raised against synthetic oligopeptide corresponding to the predicted amino acid sequence (94-108; EYGDKERKADSKMVC) of OLo [3].…”

Section: Purification Of Four Go Proteinsmentioning

confidence: 99%

“…The films were incubated with various antibodies at 30°C for 12 h and treated with biotinylated anti-rabbit IgG and streptavidine HRP. The four purified Go proteins were also ADP-ribosylated by IAP in the presence of 32p-labeled NAD as in [10][11][12]14] and followed by digestions with lysylendopeptidase as described above. The samples were electrophoresed, and the radiolabeled polypeptides were detected by autoradiography.…”

Section: Peptide Mappings Of Four Purified Go Proteins After Theirmentioning

confidence: 99%

“…GTPase activity of the purified Go proteins was assayed with various concentrations of [y-3zp]GTP in a reaction mixture consisting of 20 mM sodium N-2~hydroxyethylpiper azine-N'-2-ethanesulfonic acid (pH 7.4), 10 mM Na-EDTA and 35 mM MgCI2 at 30°C as in [11,12]. The activities are expressed as turnover rates, which normalized the activity to the maximum amounts of 3SS-labeled GTPyS binding to G proteins as in [12].…”

Section: Assay Of Gtpase Activitymentioning

confidence: 99%

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Characterization of four G_O‐type proteins purified from bovine brain membranes

Inanobe¹,

Shibasaki²,

Takahashi³

et al. 1990

FEBS Letters

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Recently we reported there were at least four types of G O or G0-1ike proteins in bovine brain membranes based on their elution profiles from Mono Q columns and their immunological reactivities; one of the proteins was purified as an ct-monomeric form, and the others as ~flT-trimers. The four proteins, of which ct-subunits were confirmed to be a family of Go-type by an immunoblot analysis, were thus referred to as %1, Go2, G03 and G04, respectively, in order of their elutions from the column. Immunostained peptide mappings arising from proteolytic digestions of the four ctsubunits, together with their fragmentation patterns containing radiolabeled ADP-ribose that had been incorporated by pertussis toxin-catalyzed ADP-ribosylation, suggested that the four G0-c~ were classified into either of two groups such as %1 and G02-c~ or Go3-C~ and Go4-C~. The kinetic parameters of their GTPase activities, however, revealed that there were different properties between %1 and Go2-c~ or Go3-c~ and Go4-a. Thus, the four G0-type proteins appeared to be different entities from one another.GTP-binding protein; Pertussis toxin (IAP); GTPase activity

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“…The ECs0 of Gs-activating function of ISRP1 was 4/IM, and the saturated effect on Gs was observed at ~ 10 ¢tM. When its concentration exceeded 30 tiM, the effect of the peptide was attenuated, which was attributed to denaturation of the G protein after strong stimulation, as described [32]. Although the Arg259-Lys273 region of ,BAR has a higher potency in the activation of Gs, it also activates Gi [28].…”

Section: Resultsmentioning

confidence: 75%

GTP‐binding protein‐activator sequences in the insulin receptor

Okamoto

Murayama

et al. 1993

FEBS Letters

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Some functions of the insulin receptor (insR) are assumed to be mediated by pertussis toxin‐sensitive Gi/Go. proteins. Here we have located G‐protein‐activator domains in the cytoplasmic region of the human insR. We searched the sequence of insR and found three candidate regions at residues 1039‐1061, 1147‐1168 and 1325‐1345, referred to as ISRP 1, ISRP2 and ISRP3, respectively. Among them, the Gi/Go‐activating function was observed only in peptide ISRP3. ISRP1 specifically activated G3, whereas ISRP2 had no effect on G proteins. ISRP2 and ISRP3 contained five of six autophosphorylated tyrosine residues in insR. After tyrosine phosphorylation, ISRP2 showed specific G1‐activating function, and ISRP3 potentiated its ability and became capable of activating G proteins generally. This is the first study that specifies G‐protein‐activator domains in insR and describes their modification by autophosphorylation.

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Wasp venom toxin mastoparan, a histamine releaser from mast cells, is a direct activator of GTP-binding regulatory proteins

Cited by 22 publications

References 15 publications

Potential roles of heterotrimeric G proteins of the endomembrane system

Potential roles of heterotrimeric G proteins of the endomembrane system

Characterization of four G_O‐type proteins purified from bovine brain membranes

GTP‐binding protein‐activator sequences in the insulin receptor

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Wasp venom toxin mastoparan, a histamine releaser from mast cells, is a direct activator of GTP-binding regulatory proteins

Cited by 22 publications

References 15 publications

Potential roles of heterotrimeric G proteins of the endomembrane system

Potential roles of heterotrimeric G proteins of the endomembrane system

Characterization of four GO‐type proteins purified from bovine brain membranes

GTP‐binding protein‐activator sequences in the insulin receptor

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Characterization of four G_O‐type proteins purified from bovine brain membranes