Elucidation of intracellular signal transductions by use of point mutated proteins and molecular tools

2016 Fiscal Year Final Research Report

• Project/Area Number: 16K13101
• Research Category: Grant-in-Aid for Challenging Exploratory Research
• Allocation Type: Multi-year Fund
• Research Field: Chemical biology
• Research Institution: Osaka University
• Principal Investigator: Kato Nobuo 大阪大学, 産業科学研究所, 教授 (50150537)
• Project Period (FY): 2016-04-01 – 2017-03-31
• Keywords: タンパク質間相互作用 / 14-3-3タンパク質 / フシコクシン / コチレニン

Outline of Final Research Achievements

14-3-3 proteins regulate intracellular signal transductions by associating with phosphorylated proteins. This study aimed to elucidate the functions of seven isoforms of human 14-3-3 protein by using their point mutants and small molecule chemical tools. The ζ isoform was used for wild type 14-3-3, and several point mutants on its Lys 120 were obtained. In any cases, the binding affinities of the point mutants toward model peptides were attenuated as compared with that of the wild type, but the association ability was partly recovered by derivatives of diterpene glycoside, fusicoccin (FC). Thus, phenotypic analysis using 14-3-3 point mutants and FC derivatives can be a useful method for functional analysis of 14-3-3 isoforms.

Free Research Field

化学生物学