Inositol polyphosphates regulate the membrane interactions of the endosomal p100, G-protein-related protein

Tatiana A. Kassessinoff , Andrew Gabet , Michael A. Beaven , Ronit Sagi-Eisenberg
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引用次数: 2

Abstract

The protein, p100, was previously identified as a G-protein related protein that cycles on and off the cytoplasmic face of the endosome membrane (Traub et al., Biochem. J. 280 (1991) 171–178). Here we present evidence that the inositol polyphosphates, inositol 1,4,5-trisphosphate (IP3) and inositol hexakisphosphate (IP6), release p100 from light-density microsomal membranes and inhibit rebinding of p100 through receptors, which are specific for IP3 or for IP6. These receptors can be co-extracted with p100 from the microsomes by 0.5 M Tris-HCl and, in the soluble state, they exhibit similar binding activity towards the inositol polyphosphates as do untreated microsomes. Soluble p100 self-aggregates and this aggregation is blocked by both IP3 and IP6. Stimulation of permeabilized rat basophilic leukemia (RBL-2H3) cells with carbachol, via transfected muscarinic m1 receptors, results in increased levels of inositol polyphosphates and the quantitative release of p100 into the cytosol. This effect is reversible and cytosolic p100 rebinds to the membrane as the levels of inositol polyphosphates decline. These findings suggest that p100 may belong to a family of IP-binding proteins whose intracellular localization is determined by extracellular signals.

肌醇多磷酸调节内体p100, g蛋白相关蛋白的膜相互作用
该蛋白p100先前被鉴定为一种g蛋白相关蛋白,在核内体膜的细胞质面上下循环(Traub et al., Biochem)。J. 280(1991) 171-178)。在这里,我们提出证据表明,肌醇多磷酸、肌醇1,4,5-三磷酸(IP3)和肌醇六磷酸(IP6)从轻密度微粒体膜释放p100,并通过IP3或IP6特异性受体抑制p100的再结合。这些受体可以用0.5 M的Tris-HCl从微粒体中与p100共同提取,并且在可溶性状态下,它们对肌醇多磷酸的结合活性与未处理的微粒体相似。可溶性p100自聚集,这种聚集被IP3和IP6阻断。通过转染的毒毒碱m1受体,用氨基苯酚刺激渗透性大鼠嗜碱性白血病(RBL-2H3)细胞,导致肌醇多磷酸水平升高,p100定量释放到细胞质中。这种作用是可逆的,随着肌醇多磷酸水平的下降,胞质p100与膜重新结合。这些发现表明p100可能属于一个ip结合蛋白家族,其细胞内定位由细胞外信号决定。
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