A simple structure encodes G protein-activating function of the IGF-II/mannose 6-phosphate receptor

Okamoto, Takashi; Katada, Toshiaki; Murayama, Yoshitake; Ui, Michio; Ogata, Etsuro; Nishimoto, Ikuo

doi:10.1016/0092-8674(90)90116-v

Cited by 275 publications

(137 citation statements)

References 40 publications

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“…For example, a G protein can couple to the insulin-like growth factor-II/mannose 6-phosphate receptor [13], G~o can be associated with a nerve growth cone protein, GAP-43 [14,15], and a pertussis toxin-sensitive G protein has been implicated in neural growth via interaction with a neural cell adhesion molecule and N-cadherin [16]. G=i has also been detected in organelles other than the plasma membrane (e.g.…”

Section: Discussionmentioning

confidence: 99%

Interaction of the protein nucleobindin with G_αi2, as revealed by the yeast two‐hybrid system

et al. 1995

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The heterotrimeric G protein, G~i2, transduces signals from seven membrane spanning receptors to effectors such as adenylyl cyclase and ion channels. The purpose of this study was to identify these or other cellular proteins that interact with G,d2 by use of the yeast two-hybrid system. A human B cell cDNA library was screened by this system using full length Gin2. Four positive colonies were obtained. Two of the four were identified as nucleobindin, a calcium binding protein and a putative antigen to which anti-nuclear antibodies are generated in mice with a disorder that resembles systemic lupus erythematosus. Nucleobindin has a leucinc zipper, EF hands, and a signal peptide sequence and is thought to localize to the nucleus as well as being secreted. The specificity of intehraction between G~2 and nucleobindin was confirmed by an in vitro binding assay using recombinant proteins. Transfeetion of Gai2 and nucleobindin in COS cells increased G~i2 expression relative to cells transfected with Goi2 and mock vector. Our results indicate that the yeast two-hybrid system provides a means to identify novel proteins that interact with G,~ proteins. Nucleobindin appears to represent one of those proteins.

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Section: Discussionmentioning

confidence: 99%

Interaction of the protein nucleobindin with G_αi2, as revealed by the yeast two‐hybrid system

et al. 1995

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“…In addition, receptors other than those with seven transmembrane domains have been predicted to couple directly to heterotrimeric G proteins. Among them is the single membrane spanning mannose-6-phosphate (M6P)/IGF II receptor which was demonstrated to couple directly to Gi2 proteins [62].…”

Section: What Are the Upstream Signaling Partners Of Organelle-associmentioning

confidence: 99%

Potential roles of heterotrimeric G proteins of the endomembrane system

Nürnberg

Ahnert‐Hilger

1996

FEBS Letters

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“…IGF-II binding has not been shown to induce phosphorylation of its receptor, but it has been suggested that IGF-II causes IGF-II͞M-6-P receptor redistribution by a mechanism involving okadaic acid-sensitive Ser͞Thr protein phosphatases (12). The fact that the cytoplasmic tail of the IGF-II͞M-6-P receptor lacks a kinase domain has prompted the suggestion that this receptor mediates its signaling through heterotrimeric GTPbinding proteins (13,14). By using the nonhydrolyzable GTP analogue GTP-␥-S, it was possible to show that cytosolic recycling of IGF-II͞M-6-P receptors to the trans-Golgi network depends on GTP hydrolysis (15).…”

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confidence: 99%

Insulin-like growth factor II signaling through the insulin-like growth factor II/mannose-6-phosphate receptor promotes exocytosis in insulin-secreting cells

Zhang

Tally

Larsson

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

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The insulin-like growth factor II (IGF-II)͞ mannose-6-phosphate (M-6-P) receptor is known to participate in endocytosis as well as sorting of lysosomal enzymes and is involved in membrane trafficking through rapid cycling between cytosolic membrane compartments and the plasma membrane. Here we demonstrate that IGF-II, acting through the IGF-II͞M-6-P receptor, promotes exocytosis of insulin in the pancreatic ␤ cell. The effect of IGF-II was evoked at nonstimulatory concentrations of glucose, was mediated by a pertussis toxin sensitive GTP-binding protein, was dependent on protein kinase C-induced phosphorylation, and was independent of changes in cytoplasmic free Ca 2؉ concentration. Since the applied concentration of IGF-II is within the range normally found free in circulation in humans, this novel signaling pathway for the IGF-II͞M-6-P receptor is likely to be involved in modulation of insulin exocytosis under physiological conditions.

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A simple structure encodes G protein-activating function of the IGF-II/mannose 6-phosphate receptor

Cited by 275 publications

References 40 publications

Interaction of the protein nucleobindin with G_αi2, as revealed by the yeast two‐hybrid system

Interaction of the protein nucleobindin with G_αi2, as revealed by the yeast two‐hybrid system

Potential roles of heterotrimeric G proteins of the endomembrane system

Insulin-like growth factor II signaling through the insulin-like growth factor II/mannose-6-phosphate receptor promotes exocytosis in insulin-secreting cells

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A simple structure encodes G protein-activating function of the IGF-II/mannose 6-phosphate receptor

Cited by 275 publications

References 40 publications

Interaction of the protein nucleobindin with Gαi2, as revealed by the yeast two‐hybrid system

Interaction of the protein nucleobindin with Gαi2, as revealed by the yeast two‐hybrid system

Potential roles of heterotrimeric G proteins of the endomembrane system

Insulin-like growth factor II signaling through the insulin-like growth factor II/mannose-6-phosphate receptor promotes exocytosis in insulin-secreting cells

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Interaction of the protein nucleobindin with G_αi2, as revealed by the yeast two‐hybrid system

Interaction of the protein nucleobindin with G_αi2, as revealed by the yeast two‐hybrid system