(Last updated : 2024-09-04 09:45:30)
  MOCHIZUKI, Takahiro
   Department   Aoyama Gakuin University  Department of Chemistry and Biological Science, College of Science and Engineering
   Position   Assistant Professor
■ Specialization and related fields
Molecular biology 
■ Business career
1. 2016/04~2017/03 Aoyama Gakuin University College of Science and Engineering Department of Chemistry and Biological Science Research Associate
2. 2017/04~2020/08 Aoyama Gakuin University College of Science and Engineering Department of Chemistry and Biological Science Assistant Professor
3. 2024/09~ Aoyama Gakuin University College of Science and Engineering Department of Chemistry and Biological Science Assistant Professor
■ Research topic, funded research, and department laboratory expense
1. 2016/10~2018/03  A new regulatory mechanism of the yeast amino acid permease by phosphorylation  (Key Word : )
■ Book and thesis
1. Article Functional analysis of human aromatic amino acid transporter MCT10/TAT1 using the yeast Saccharomyces cerevisiae.   (Collaboration) 2017/10
2. Article Retention of chimeric Tat2-Gap1 permease in the endoplasmic reticulum induces unfolded protein response in Saccharomyces cerevisiae   (Collaboration) 2015
3. Article Functional mapping and implications of substrate specificity of the yeast high-affinity leucine permease Bap2.   (Collaboration) 2014
4. Article The loss of hydroxyl groups from the ceramide moiety leads to a reduction in the lateral diffusion of membrane proteins in Saccharomyces cerevisiae.   (Collaboration) 2014
5. Article Pressure-induced endocytic degradation of the yeast low-affinity tryptophan permease Tat1 is mediated by Rsp5 ubiquitin ligase and functionally redundant PPxY-motif proteins.   (Collaboration) 2013
■ Academic conference presentation
1. 2018/09 Exploration of high-pressure sensor proteins in the yeast saccharomyces cerevisiae (10th International Conference on High Pressure Bioscience and Biotechnology)
2. 2018/09 Phosphorylation of the yeast tryptophan permease Tat1 mediates its ubiquitin-dependent degradation in response to high pressure. (10th International Conference on High Pressure Bioscience and Biotechnology)