当前位置: X-MOL 学术J. Biol. Chem. › 论文详情
Competition between two high- and low-affinity protein-binding sites in myosin VI controls its cellular function
Journal of Biological Chemistry ( IF 4.106 ) Pub Date : 2020-01-10 , DOI: 10.1074/jbc.ra119.010142
Natalia Fili, Yukti Hari-Gupta, Bjork Aston, Ália dos Santos, Rosemarie E. Gough, Bana Alamad, Lin Wang, Marisa L. Martin-Fernandez, Christopher P. Toseland

Myosin VI is involved in many cellular processes ranging from endocytosis to transcription. This multifunctional potential is achieved through alternative isoform splicing and through interactions of myosin VI with a diverse network of binding partners. However, the interplay between these two modes of regulation remains unexplored. To this end, we compared two different binding partners and their interactions with myosin VI by exploring the kinetic properties of recombinant proteins and their distribution in mammalian cells using fluorescence imaging. We found that selectivity for these binding partners is achieved through a high-affinity motif and a low-affinity motif within myosin VI. These two motifs allow competition among partners for myosin VI. Exploring how this competition affects the activity of nuclear myosin VI, we demonstrate the impact of a concentration-driven interaction with the low-affinity binding partner DAB2, finding that this interaction blocks the ability of nuclear myosin VI to bind DNA and its transcriptional activity in vitro. We conclude that loss of DAB2, a tumor suppressor, may enhance myosin VI–mediated transcription. We propose that the frequent loss of specific myosin VI partner proteins during the onset of cancer leads to a higher level of nuclear myosin VI activity.
更新日期:2020-01-11

 

全部期刊列表>>
化学/材料学中国作者研究精选
Springer Nature 2019高下载量文章和章节
《科学报告》最新环境科学研究
ACS材料视界
自然科研论文编辑服务
中南大学国家杰青杨华明
剑桥大学-
中国科学院大学化学科学学院
材料化学和生物传感方向博士后招聘
课题组网站
X-MOL
北京大学分子工程苏南研究院
华东师范大学分子机器及功能材料
中山大学化学工程与技术学院
试剂库存
天合科研
down
wechat
bug