Myotubularin related protein 7, a novel STIM1 binding protein.

IF 1.7 4区 医学 Q3 PHARMACOLOGY & PHARMACY
Ning Dai, Jody Groenendyk, Marek Michalak
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引用次数: 0

Abstract

Stromal interaction molecule 1 (STIM1) is a Ca2+ sensor in the endoplasmic reticulum (ER) membrane. The protein plays a crucial role in store-operated Ca2+ entry (SOCE) by transducing ER Ca2+ depletion signals to Ca2+ release-activated Ca2+ channel protein 1 (ORAI1) at the plasma membrane. Myotubularin related protein 7 (MTMR7) is a lipid phosphatase that dephosphorylates phosphoinositides. Using yeast two-hybrid analysis, immunoprecipitation and fluorescence microscopy, we discovered that MTMR7 interacts with STIM1 at the ER. These observations identified MTMR7 as a novel STIM1-binding protein that bridges myotubularins and phosphoinositide signaling with SOCE. Our research revealed a novel link between Ca2+ signaling and phosphoinositide biology, positioning MTMR7 as a potential marker or drug target for SOCE related human pathophysiology.

肌小管蛋白相关蛋白7,一种新的STIM1结合蛋白。
基质相互作用分子1 (STIM1),内质网(ER)膜上的Ca2+传感器。该蛋白通过将ER Ca2+耗竭信号转导至质膜上Ca2+释放激活的Ca2+通道蛋白1 (ORAI1),在储存操作Ca2+进入(SOCE)中起着至关重要的作用。肌小管蛋白相关蛋白7 (MTMR7)是一种脂质磷酸酶,可使磷酸肌苷去磷酸化。通过酵母双杂交分析、免疫沉淀和荧光显微镜,我们发现MTMR7在ER处与STIM1相互作用。这些观察结果表明,MTMR7是一种新的stim1结合蛋白,通过SOCE连接肌小管蛋白和磷酸肌苷信号。我们的研究揭示了Ca2+信号和磷酸肌苷生物学之间的新联系,将MTMR7定位为SOCE相关人类病理生理学的潜在标记物或药物靶点。
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来源期刊
CiteScore
4.00
自引率
4.80%
发文量
90
审稿时长
3-8 weeks
期刊介绍: Published since 1929, the Canadian Journal of Physiology and Pharmacology is a monthly journal that reports current research in all aspects of physiology, nutrition, pharmacology, and toxicology, contributed by recognized experts and scientists. It publishes symposium reviews and award lectures and occasionally dedicates entire issues or portions of issues to subjects of special interest to its international readership. The journal periodically publishes a “Made In Canada” special section that features invited review articles from internationally recognized scientists who have received some of their training in Canada.
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