Kyushu University Academic Staff Educational and Research Activities Database
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SHIGEHIKO TAMURA Last modified date:2018.06.15



Graduate School
Undergraduate School


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
Papers
1. SHIGEHIKO TAMURA, Naomi Matsumoto, Ryota Takeba, Yukio Fujiki, AAA Peroxins and Their Recruiter Pex26p Modulate the Interactions of Peroxins Involved in Peroxisomal Protein Import., J. Biol. Chem., doi: 10.1074/jbc.M114.588038., 289, (35), 24336-24346, 2014.08, Pex1p and Pex6p are required for the relocation of the import
receptor Pex5p from the peroxisomal membrane to the cytosol.
Weherein show that mammalian Pex26p directly binds to Pex14p,
the initial docking receptor of Pex5p, and interacts with Pex5p via
Pex14p. The binding affinity of Pex26p to Pex14p is altered by
Pex5p. Further evidence suggests that the N-terminal region in
Pex26p acts as a scaffold protein to recruit Pex14pPex5p complex
together with Pex1pPex6p complexes on peroxisomes. Pex26p
binding to Pex14p was suppressed by overexpression of Pex1p and
Pex6p in an ATP-dependent manner, whereas Pex14p was not
competed out by Pex1p and Pex6p from Pex26p mutant defective
in peroxisomal matrix protein import. These results suggested that
peroxisome biogenesis requires Pex1p- and Pex6p-regulated dissociation
of Pex14p from Pex26p. Pex1p homo-oligomer directly
binds to Pex5p as assessed by a surface plasmon resonance-based
assay. Moreover, cytosolic Pex1p is likely to maintain the functional
oligomer of Pex5p. Taken together, in the peroxisomal protein
import, AAA peroxins modulate the interaction between
Pex26p and Pex14p on peroxisome membrane as well as Pex5p
oligomer in the cytosol..
Presentations
1. Peroxisomal matrix protein import: Identification of core components of membrane translocator..
2. Peroxisomal matrix protein transport requires a series of constitutional changes of Pex14p homo-oligomers..
3. 田村 茂彦, 河村優子, 藤木幸夫, Identification of core components of peroxisomal membrane translocator., 第89回日本生化学会, 2016.09, Peroxisomal matrix proteins are imported into peroxisomes via membrane-bound docking/translocation complex comprising as a major component membrane peroxin Pex14p that binds Pex5p, a peroxisomal targeting signal type-1 (PTS1) receptor. However, molecular mechanism underlying peroxisome matrix protein import remains elusive, because components and their functional roles of the docking/translocation complex are little defined.
We very recently isolated by BN-PAGE method as a docking/translocation complex three types of Pex14p complexes, termed complexes I, II, and III, with molecular masses 600 kDa, 770 kDa, and 1,100 kDa, respectively. The complex I is assembled as a dodecamer of Pex14p. The complexes II and III contain Pex5p, while Pex13p is required only for assembly of the complex III. The complex III dissociates into the complex II by interacting with either Pex5p or Pex5p-PTS1 cargo complexes. Moreover, Pex5p binding to PTS1-cargo protein enhances the dissociation of complex III. Transition of Pex14p complex structures between complexes I, II, and III more likely plays important roles in matrix protein import. On the other hand, complex I binds to Pex5p, not Pex5p-PTS1 cargo complexes, suggesting that the complex III is responsible for the peroxisome matrix protein import. Taken together, peroxisomal protein transport correlates well with the dissociation of complex III which is a translocator complex consisted of Pex14p. We will discuss potential roles of the peroxisomal docking/translocation complex in matrix protein transport..
4. Identification of core components of peroxisomal membrane translocator.
5. Identification of core components of peroxisomal membrane translocator..
6. AAA peroxins and their recruiter Pex26p modulate the peroxin interactions involved in peroxisomal protein import.
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
Social
Professional and Outreach Activities
nothing.