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全长和截短型人ZIP4锌转运蛋白在……中的异源表达

Heterologous Expression of Full-Length and Truncated Human ZIP4 Zinc Transporter in .

作者信息

Liu Yuting, Bafaro Elizabeth M, Dempski Robert E

机构信息

Department of Chemistry and Biochemistry, Worcester Polytechnic Institute, Worcester, MA 01609, USA.

出版信息

Biomolecules. 2022 May 21;12(5):726. doi: 10.3390/biom12050726.

DOI:10.3390/biom12050726
PMID:35625653
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9138318/
Abstract

The human (h) transporter hZIP4 is the primary Zn importer in the intestine. hZIP4 is also expressed in a variety of organs such as the pancreas and brain. Dysfunction of hZIP4 can result in the Zn deficiency disease acrodermatitis enteropathica (AE). AE can disrupt digestive and immune system homeostasis. A limited number of hZIP4 expression strategies have hindered increasing knowledge about this essential transmembrane protein. Here, we report the heterologous expression of hZIP4 in . Both a wild-type and a mutant strain, in which the endogenous Zn transporters were deleted, were used to test the expression and localization of an hZIP4-GFP fusion protein. A full-length hZIP4-GFP and a truncated membrane-domain-only (mhZIP4-GFP) protein were observed to be present in the plasma membrane in yeast.

摘要

人类(h)转运蛋白hZIP4是肠道中主要的锌导入体。hZIP4也在多种器官中表达,如胰腺和大脑。hZIP4功能失调可导致锌缺乏疾病肠病性肢端皮炎(AE)。AE会破坏消化系统和免疫系统的稳态。hZIP4表达策略的有限性阻碍了对这种重要跨膜蛋白的深入了解。在此,我们报道了hZIP4在……中的异源表达。使用野生型和内源性锌转运体被缺失的突变株来测试hZIP4-GFP融合蛋白的表达和定位。在酵母中观察到全长hZIP4-GFP和仅截短的膜结构域(mhZIP4-GFP)蛋白存在于质膜中。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d93b/9138318/be8271cc1f51/biomolecules-12-00726-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d93b/9138318/e58fd3d66830/biomolecules-12-00726-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d93b/9138318/c58f56a1bae2/biomolecules-12-00726-g002a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d93b/9138318/cc3f7dd50702/biomolecules-12-00726-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d93b/9138318/be8271cc1f51/biomolecules-12-00726-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d93b/9138318/e58fd3d66830/biomolecules-12-00726-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d93b/9138318/c58f56a1bae2/biomolecules-12-00726-g002a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d93b/9138318/cc3f7dd50702/biomolecules-12-00726-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d93b/9138318/be8271cc1f51/biomolecules-12-00726-g004.jpg

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本文引用的文献

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Overproduction of Human Zip (SLC39) Zinc Transporters in for Biophysical Characterization.用于生物物理特性分析的人类 Zip(SLC39)锌转运蛋白过表达。
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Elucidating the H Coupled Zn Transport Mechanism of ZIP4; Implications in Acrodermatitis Enteropathica.阐明 ZIP4 的 H 偶联 Zn 转运机制;在肠病性肢端皮炎中的意义。
Int J Mol Sci. 2020 Jan 22;21(3):734. doi: 10.3390/ijms21030734.
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Quantifying the Oligomeric State of hZIP4 on the Surface of Cells.量化细胞表面hZIP4的寡聚状态。
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Crystal structures of a ZIP zinc transporter reveal a binuclear metal center in the transport pathway.ZIP 锌转运蛋白的晶体结构揭示了运输途径中的双核金属中心。
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Adapted Treatment Guided by Interim PET-CT Scan in Advanced Hodgkin's Lymphoma.基于中期PET-CT扫描指导的晚期霍奇金淋巴瘤适应性治疗
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Structural insights of ZIP4 extracellular domain critical for optimal zinc transport.ZIP4 细胞外结构域的结构见解对最佳锌转运至关重要。
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Computation and Functional Studies Provide a Model for the Structure of the Zinc Transporter hZIP4.计算和功能研究为锌转运蛋白hZIP4的结构提供了一个模型。
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