Researcher Database

（Last updated : 2024-10-21 13:25:10）　

SHIRAKABE KYOKO

Department / Course College of Life Sciences Department of Biomedical Sciences

Title / Position Professor

Other Affiliations
1.	Research Organization of Science and Technology Center for Systems Vision Science
2.	Graduate School of Life Sciences

Academic background
1.	～1997/05	Doctoral Program (2nd Semester) │ Department of Biophysics │ Graduate School of Science │ Kyoto University │ Completed Ph.D. (Science)
2.	～1994/03	Master Course │ Department of Biochemistry and Biophysics │ Graduate School of Science │ The University of Tokyo │ Completed
3.	～1992/03	Department of Biochemistry │ Faculty of Science │ The University of Tokyo │ Graduated

Research activities
1.		Japan Human Proteome Organisation
2.		Japan Society of Cell Biology
3.		The Japanese Biochemical Society
4.		Japan Society for Proteases in Pathophysiology
5.		The Molecular Biology Society of Japan

Subject of research
1.	Roles of Protein Modifications in Disease Onset

Research summary
Roles of Protein Modifications in Disease Onset Post-translational modification is indispensable for living organisms to adapt to a changing environment, and its breakdown causes several diseases including cancer. We focus on a post-translational modification called“ectodomain shedding (shedding)”, which liberates the extracellular domain of membrane proteins through juxtamembrane processing. Shedding can not only release growth factors and cytokines, but also decrease the amount of cell surface receptors and adhesion molecules. Through these processing events, shedding can fundamentally regulate cell-cell communications, but its regulatory mechanisms and physiological functions remain largely elusive. We are using proteomics approach to enrich our understanding about shedding.

Present specialized field
Tumor biology, Molecular biology, Functional biochemistry, Cell biology, General medical chemistry, Pathological medical chemistry, Immunology (Keyword：Membrane proteins, ADAM family metalloproteases, Ectodomain shedding, Alternative splicing, Cancer, Signal transduction, Inflammation)

Papers
1.	2024/02/12	C-terminal amino acids in the type I transmembrane domain of L-type lectin VIP36 affect g-secretase susceptibility │ Biochemical and Biophysical Research Communications │ 696 (Co-authored)
2.	2020	Negatively charged amino acids in the stalk region of membrane proteins reduce ectodomain shedding. │ J Biol Chem. │ in press
3.	2019/06	LRRK1 phosphorylation of Rab7 at S72 links trafficking of EGFR-containing endosomes to its effector RILP │ J Cell Sci │ 132 (11)
4.	2019/01	プロテオーム解析から明らかになったシェディングの役割と制御機構、化学と生物 │ ,pp.15-20
5.	2017	Mechanistic insights into ectodomain shedding: susceptibility of CADM1 adhesion molecule is determined by alternative splicing and O-glycosylation │ Sci Rep. │ 7,pp.46174
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Academic conference presentation
1.	2024/05/14	Analysis of molecular mechanisms determining susceptibility to ectodomain shedding (Proteolysis at the membrane - from signaling to disease)
2.	2023/06/27	PROTEOMIC APPROACHES TO MEMBRANE PROTEIN PROCESSING (12th General Meeting of the International Proteolysis Society)
3.	2022/11/30	Analysis of phosphorylation using Rab7 mutants
4.	2022/11/30	Amino acid of sequence transmembrane domain of VIP36 determines the susceptibility of RIP (regulated inteamembrane proteolysis)
5.	2022/11/30	Comparison of the function of SIRPα splicing variants in intercellular communication
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E-Mail Address

Department laboratory expense researcher number
00345315

researchmap Researcher code
5000036305