Golgin45-Syntaxin5 Interaction Contributes to Structural Integrity of the Golgi Stack

doi:10.1038/s41598-019-48875-x

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	Golgin45-Syntaxin5 Interaction Contributes to Structural Integrity of the Golgi Stack
	Tiwari, Neeraj 1; Graham, Morven 1; Liu, Xinran 1; Yue, Xihua2 ; Zhu, Lianhui2 ; Meshram, Dipak2 ; Choi, Sunkyu2 ; Qian, Yi2 ; Rothman, James E.1; Lee, Intaek2
	2019-08-28
发表期刊	SCIENTIFIC REPORTS (IF:3.8[JCR-2023],4.3[5-Year])
ISSN	2045-2322
卷号	9
发表状态	已发表
DOI	10.1038/s41598-019-48875-x
摘要	The unique stacked morphology of the Golgi apparatus had been a topic of intense investigation among the cell biologists over the years. We had previously shown that the two Golgin tethers (GM130 and Golgin45) could, to a large degree, functionally substitute for GRASP-type Golgi stacking proteins to sustain normal Golgi morphology and function in GRASP65/55-double depleted HeLa cells. However, compared to well-studied GM130, the exact role of Golgin45 in Golgi structure remains poorly understood. In this study, we aimed to further characterize the functional role of Golgin45 in Golgi structure and identified Golgin45 as a novel Syntaxin5-binding protein. Based primarily on a sequence homology between Golgin45 and GM130, we found that a leucine zipper-like motif in the central coiled-coil region of Golgin45 appears to serve as a Syntaxin5 binding domain. Mutagenesis study of this conserved domain in Golgin45 showed that a point mutation (D171A) can abrogate the interaction between Golgin45 and Syntaxin5 in pull-down assays using recombinant proteins, whereas this mutant Golgin45 binding to Rab2-GTP was unaffected in vitro. Strikingly, exogenous expression of this Syntaxin5 binding deficient mutant (D171A) of Golgin45 in HeLa cells resulted in frequent intercisternal fusion among neighboring Golgi cisterna, as readily observed by EM and EM tomography. Further, double depletion of the two Syntaxin5-binding Golgin tethers also led to significant intercisternal fusion, while double depletion of GRASP65/55 didn't lead to this phenotype. These results suggest that certain tether-SNARE interaction within Golgi stack may play a role in inhibiting intercisternal fusion among neighboring cisternae, thereby contributing to structural integrity of the Golgi stack.
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收录类别	SCI ; SCIE
语种	英语
WOS研究方向	Science & Technology - Other Topics
WOS类目	Multidisciplinary Sciences
WOS记录号	WOS:000482886700019
出版者	NATURE PUBLISHING GROUP
WOS关键词	MATRIX PROTEIN ; FRAGMENTATION ; KINASE ; GM130
原始文献类型	Article
引用统计	正在获取...
文献类型	期刊论文
条目标识符	https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/79734
专题	生命科学与技术学院_特聘教授组_James E. Rothman组
通讯作者	Lee, Intaek
作者单位	1.Yale Univ, Sch Med, Dept Cell Biol, New Haven, CT 06520 USA 2.ShanghaiTech Univ, Sch Life Sci & Technol, Shanghai, Peoples R China
通讯作者单位	生命科学与技术学院
推荐引用方式 GB/T 7714	Tiwari, Neeraj,Graham, Morven,Liu, Xinran,et al. Golgin45-Syntaxin5 Interaction Contributes to Structural Integrity of the Golgi Stack[J]. SCIENTIFIC REPORTS,2019,9.
APA	Tiwari, Neeraj.,Graham, Morven.,Liu, Xinran.,Yue, Xihua.,Zhu, Lianhui.,...&Lee, Intaek.(2019).Golgin45-Syntaxin5 Interaction Contributes to Structural Integrity of the Golgi Stack.SCIENTIFIC REPORTS,9.
MLA	Tiwari, Neeraj,et al."Golgin45-Syntaxin5 Interaction Contributes to Structural Integrity of the Golgi Stack".SCIENTIFIC REPORTS 9(2019).