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The Distribution of Synaptotagmin Ⅱ in RBL-2H3 and Its Regulation on Exocytosis of Lysosomes in RBL-2H3

Cellular & Molecular Immunology 2005年第3期2卷 205-209页

作者： Jicheng Zhang Jianmin Wu Shixiu Pan Wenli Lv Department of Medical Laboratory Union Hospital Tongji MedicalCollege Huazhong University of Science and Technology Wuhan 430022China Wuhan Institute of Biological Products Wuhan 430060 China

Synaptotagmin （Syt） constitutes a family of membrane-trafficking proteins, so far nearly 20 Syts have been discovered. Extensive work showed that synatotagmins were a potential Ca^2＋ sensor for regulated exocytosis. This study was to investigate the expression and location of synaptotagmin II （Syt2） in RBL-2H3 （RBL） and its role in regulating exocytosis of RBL. The expression of Syt2 in RBL was confirmed by Western blot. The recombinant expression vector pEGFP-N1-Syt2 was constructed and transfected into RBL by electroporation, the stable transfectant RBL-Syt2-S expressing fusion protein Syt2-EGFP were obtained and Syt2 was highly concentrated at plasma membrane with little detected in cytoplasm. To analyze the role of Syt2 during exocytosis of RBL, the release of cathepsin D was assayed by immunoblotting. Compared with control, the release of cathepsin D by RBL-Syt2-S was markedly decreased. The results indicated that Syt2 played a negative regulation in exocytosis of lysosomes in RBL. Cellular ＆ Molecular Immunology. 2005;2（3）：205-209.

关键词： calcium binding protein mast cell gene expression lysosome exocytosis

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The Ca2+ sensor SCaBP3 Fine Tunes Arabidopsis Saline-alkali Tolerance by Modulating Plasma Membrane H+-ATPase Activity

The Ca2+ sensor SCaBP3 Fine Tunes Arabidopsis Saline-alkali ...

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2018全国植物生物学大会

作者： Yujiao Wu Yongqing Yang Yan Guo State Key Laboratory of Plant Physiology and Biochemistry College of Biological SciencesChina Agricultural University

Plasma membrane(PM) H-ATPases play an important role in the establishment of trans-plasma membrane pH gradient to support ion and metabolite *** Cterminal autoinhibitory domain is critical for the regulation of PM H-ATPase activity;however the underlying mechanism is not well ***,we report that the C terminus and the Centerloop region of the PM H-ATPase interact with each other,and that interaction of the SCaBP3 with the RI domain of the C terminus further enhances this interaction,this in turn promotes its autoinhibition to the PM H-ATPase ***,Arabidopsis SCaBP3 loss-of-function plants exhibit increased PM H-ATPase ***,SCaPB3 interacts with the SOS2 like protein kinase5(PKS5),a negative regulator of PM H-ATPase,and also enhances the interaction between PM H-ATPase AHA2 and *** plant and yeast systems,SCaBP3 augments PKS5 mediated inhibition of the PM *** together,our results suggest that the C-terminal autoinhibition of PM H-ATPase is at least partially established through directly interacting with the Centerloop region,and that SCaBP3/CBL7 plays a critical role in enahncing or stabilizing the repression of PM H-ATPase activity by simultaneously promoting the interaction between the C terminus and Centerloop and between the C terminus and PKS5.

关键词： plasma membrane H+-ATPase kinase calcium binding protein

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