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SHIGEHIKO TAMURA Last modified date：2023.11.28

Professor / Division for Experimental Natural Science
Faculty of Arts and Science


Graduate School
Department of Systems Life Sciences
Graduate School of Systems Life Sciences
Undergraduate School
Department of Biology
School of Sciences


Homepage
https://kyushu-u.elsevierpure.com/en/persons/shigehiko-tamura
　Reseacher Profiling Tool　Kyushu University Pure
Academic Degree
Ph.D
Country of degree conferring institution (Overseas)
No
Field of Specialization
Molecular Cellular Biology
Total Priod of education and research career in the foreign country
02years06months
Research
Research Interests
  • Molecular analysis of peroxisomal biogenesis and its pathogenesis.
    keyword : peroxisome, AAA-ATPase, protein translocator complex, peroxisome biogenesis disorder
    1996.02.
Academic Activities
Reports
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Papers
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1. Koichiro Yamashita, Shigehiko Tamura, Masanori Honsho, Hiroto Yada, Yuichi Yagita, Hidetaka Kosako, Yukio Fujiki, Mitotic phosphorylation of Pex14p regulates peroxisomal import machinery, Journal of Cell Biology, 10.1083/JCB.202001003, 219, 10, 2020.10, © 2020 Yamashita et al. Peroxisomal matrix proteins are imported into peroxisomes via membrane-bound docking/translocation machinery. One central component of this machinery is Pex14p, a peroxisomal membrane protein involved in the docking of Pex5p, the receptor for peroxisome targeting signal type 1 (PTS1). Studies in several yeast species have shown that Pex14p is phosphorylated in vivo, whereas no function has been assigned to Pex14p phosphorylation in yeast and mammalian cells. Here, we investigated peroxisomal protein import and its dynamics in mitotic mammalian cells. In mitotically arrested cells, Pex14p is phosphorylated at Ser-232, resulting in a lower import efficiency of catalase, but not the majority of proteins including canonical PTS1 proteins. Conformational change induced by the mitotic phosphorylation of Pex14p more likely increases homomeric interacting affinity and suppresses topological change of its N-terminal part, thereby giving rise to the retardation of Pex5p export in mitotic cells. Taken together, these data show that mitotic phosphorylation of Pex14p and consequent suppression of catalase import are a mechanism of protecting DNA upon nuclear envelope breakdown at mitosis..
Presentations
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1. Regulation of peroxisomal import by mitotic phosphorylation of Pex14p..
2. A newly identified mutation in the PEX26 gene is associated with a distinctly milder form of Zellweger spectrum disorder..
3. A newly identified mutation in the PEX26 gene is associated with a distinctly milder form of Zellweger spectrum disorder.
4. Mitotic regulation of peroxisomal import machinery by phosphorylation of Pex14p.
5. Regulation of peroxisomal import machinery by cell-cycle dependent phosphorylation of Pex14p.
Membership in Academic Society
  • The Japanese Biochemical Society
  • The Pharmaceutical Society of Japan
  • The Molecular Biology society of Japan
  • Japan Society for Cell Biology
Educational
Educational Activities
Life Science A
Biochemistry
Cell Biology
Seminar for metabolic physiology


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