检索结果-南通市图书馆

Interactions between Transmembrane Helices within Monomers of the Aquaporin AtPIP2;1 Play a Crucial Role in tetramer formation

引用

Molecular Plant 2016年第7期9卷 1004-1017页

作者： Yun-Joo Yoo Hyun Kyung Lee Wonhee Han Dae Heon Kim Myoung Hui Lee Jouhyun Jeon Dong Wook Lee Junho Lee Yongjik Lee Juhun Lee Jin Seok Kim Yunje Cho Jin-Kwan Han Inhwan Hwang School of Interdisciplinary Bioscience and Bioengineering Pohang University of Science and Technology Pohang 790-784 Korea Department of Life Sciences Pohang University of Science and Technology Pohang 790-784 Korea Department of Biology Sunchon National University Sunchon 57922 Korea Division of Integrative Biosciences and Biotechnology Pohang University of Science and Technology Pohang 790-784 Korea

Aquaporin （AQP） is a water channel protein found in various subcellular membranes of both prokaryotic and eukaryotic cells. The physiological functions of AQPs have been elucidated in many organisms. However, understanding their biogenesis remains elusive, particularly regarding how they assemble into tetramers. Here, we investigated the amino acid residues involved in the tetramer formation of the Arabidopsis plasma membrane AQP AtPIP2;1 using extensive amino acid substitution mutagenesis. The mutant proteins V41A/ E44A, F51A/L52A, F87A/191A, F92A/193A, V95A/Y96A, and H216A/L217A, harboring alanine substitutions in the transmembrane （TM） helices of AtPIP2;1 polymerized into multiple oligomeric complexes with a vari- able number of subunits greater than four. Moreover, these mutant proteins failed to traffic to the plasma membrane, instead of accumulating in the endoplasmic reticulum （ER）. Structure-based modeling revealed that these residues are largely involved in interactions between TM helices within monomers. These results suggest that inter-TM interactions occurring both within and between monomers play crucial roles in tetramer formation in the AtPIP2;1 complex. Moreover, the assembly of AtPIP2;1 tetramers is critical for their trafficking from the ER to the plasma membrane, as well as water permeability.

关键词： aquaporin AtPIP2 tetramer formation interaction between transmembrane helices

来源：

维普期刊数据库评论

在线全文

维普期刊数据库

学校读者我要写书评

暂无评论

欢迎您,

建议与咨询留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

时间限定

文献类型

馆藏选择

核心期刊

语言

文献类型

帮助

文字说明：

检索规则说明：

检索范例：

分类表

所选分类

限定检索结果

文献类型

馆藏范围

日期分布

学科分类号

主题

机构

作者

语言

在线全文

请选择保存的检索档案：

请选择收藏分类：

通借通还

欢迎您,

建议与咨询 留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

时间限定

文献类型

馆藏选择

核心期刊

语言

文献类型

帮助

文字说明：

检索规则说明：

检索范例：

分类表

所选分类

限定检索结果

文献类型

馆藏范围

日期分布

学科分类号

主题

机构

作者

语言

在线全文

请选择保存的检索档案： 新增检索档案 确定 取消

请选择收藏分类： 新增自定义分类 确定 取消

通借通还

建议与咨询留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

请选择保存的检索档案：

请选择收藏分类：