研究業績

分子細胞生物学研究室

Tamura, S., Matsumoto, N., Takeba, R., and *Fujiki, Y.: AAA peroxins and their recruiter Pex26p modulate the interactions of peroxins involved in peroxisomal protein import. J. Biol. Chem. 289: 24336-24346 (2014).

Fujiki, Y., Okumoto, K., Mukai, S., and Tamura, S.: Molecular basis for peroxisome biogenesis disorders. In: Brocard, C. and Hartig, A. (eds) Molecular machines involved in peroxisome biogenesis and maintenance, Springer-Verlag, Wien, Austria. pp. 91-110 (2014).

Fujiki, Y., Okumoto, K., Mukai, S., and Tamura, S.: Molecular basis for peroxisome biogenesis disorders. In: Brocard, C. and Hartig, A. (eds) Molecular machines involved in peroxisomes maintenance, in press. Berlin, Springer-Verlag (2013).

Fujiki, Y., Nashiro, C., Miyata, N., Tamura, S., and Okumoto, K.: New insights into dynamic and functional assembly of the AAA peroxins, Pex1p and Pex6p, and their membrane receptor Pex26p in shuttling of PTS1-receptor Pex5p during peroxisome biogenesis. Biochim. Biophys, Acta -Mol. Cell Res. 1823: 145-149 (2012)

Nashiro, C., Kashiwagi, A., Matsuzaki, T., Tamura, S., and Fujiki, Y.: Recruiting mechanism of the AAA peroxins, Pex1p and Pex6p, to Pex26p on peroxisome membrane. Traffic 12: 774-788 (2011).

Su, J. R., Takeda, K., Tamura, S., Fujiki., Y., and Miki, K.: Crystal struture of the conserved N-terminal domain of the peroxisomal matrix protein import receptor, Pex14p. Proc. Natl. Acad. Sci. USA 106: 417-421 (2009).

Matsumoto, N., Tamura, S. and Fujiki, Y.: The novel pathogenic peroxin Pex26p recruits the Pex1p-Pex6p AAA ATPase complexes to peroxisomes. Nat. Cell Biol. 5, 454-460 (2003)

1) Ghaedi, K., Tamura, S., Okumoto, K., Matsuzono, Y., and Fujiki, Y. The peroxin Pex3p initiates membrane assembly in peroxisome biogenesis. Mol. Biol. Cell, 11, 2085-2102 (2000).

2) Toyama, R., Mukai, S., Itagaki, A., Tamura, S., Shimozawa, N., Suzuki, Y., Kondo, N., Wanders, R. J. A., and Fujiki, Y. Isolation, characterization, and mutation analysis of PEX13-defective Chinese hamster ovary cell mutants. Hum. Mol. Genet. 8, 1673-1681 (1999).

3) Ghaedi, K., Itagaki, A., Toyama, R., Tamura, S., Matsumura, T., Kawai, A., Shimozawa, N., Suzuki, Y., Kondo, N., and Fujiki, Y. Newly identified Chinese hamster ovary cell mutants defective in peroxisome assembly represent complementation group A of human peroxisome biogenesis disorders and one novel group in mammals. Exp. Cell Res. 248, 482-488 (1999).

6) Shimizu, N., Itoh, R., Hirono, H., Otera, H., Ghaedi, K., Tateishi, K., Tamura, S., Okumoto, K., Harano, T., Mukai, S., and Fujiki, Y. The Peroxin Pex14p: cDNA cloning by functional complementation on a Chinese hamster ovary cell mutant, characterization, and functional analysis. J. Biol. Chem. 274, 12593-12604 (1999).

7) Matsuzono, Y., Kinoshita, N., Tamura, S., Shimozawa, N., Hamasaki, M., Ghaedi, K., Wanders, R. J. A., Suzuki, Y., Kondo, N., and Fujiki, Y. Human PEX19: cDNA cloning by functional complementation, mutation analysis in a Zellweger patient, and potential role in peroxisomal membrane assembly. Proc. Natl. Acad. Sci. USA. 96, 2116-2121 (1999).

8) Honsho, M., Tamura, S., Shimozawa, N., Suzuki, Y., Kondo, N., and Fujiki, Y. Mutation in PEX16 is causal in the peroxisome-deficient Zellweger syndrome of complementation group D. Am. J. Hum. Genet. 63, 1622-1630 (1998)

9) Imamura, A., Tamura, S., Shimozawa, N., Suzuki, Y., Zhang, Z., Tsukamoto, T., Orii, T., Kondo, N., Osumi, T., and Fujiki, Y. Temperature-sensitive mutation in PEX1 moderates the phenotypes of peroxisome deficiency disorders. Hum. Mol. Genet. 7, 2089-2094 (1998)

10) Okumoto, K., Shimozawa, N., Kawai, A., Tamura, S., Tsukamoto, T., Osumi, T., Moser, H., Wanders, R.J.A., Suzuki, Y., Kondo, N. and Fujiki, Y. PEX12, the pathogenic gene of group III Zellweger syndrome: cDNA cloning by functional complementation on a CHO cell mutant, patient analysis, and characterization of Pex12p. Mol. Cell. Biol. 18, 4324-4336. (1998)

11) Tamura, S., Shimozawa, N., Suzuki, Y., Tsukamoto, T., Osumi, T. and Fujiki, Y. A cytoplasmic AAA family peroxin, Pex1p, interacts with Pex6p. Biochem. Biophys. Res. Commun. 245, 883-886. (1998)

12) Tamura, S., Okumoto, K., Toyama, R., Shimozawa, N., Tsukamoto, T., Suzuki, Y., Osumi, T., Kondo, N. and Fujiki, Y. Human PEX1 cloned by functional complementation on a CHO cell mutant is responsible for peroxisome-deficient Zellweger syndrome of complementation group I. Proc. Natl. Acad. Sci. USA. 95, 4350-4355. (1998)

13) Tamura, S., Nelson, H., Tamura, A. and Nelson, N. Short external loops as potential substrate binding site of GABA transporters. J. Biol. Chem. 270, 28712-28715. (1995)

14) Jursky, F., Tamura, S., Tamura, A., Mandiyan, S., Nelson, H. and Nelson, N. Structure, function and brain localization of neurotransmitter transporters. J. Exp. Biol. 196, 283-295. (1994)

15) Tamura, S., Wang, XH., Maeda, M. and Futai, M. Gastric DNA-binding proteins recognize upstream sequence motifs of parietal cell specific genes. Proc. Natl. Acad. Sci. USA. 90, 10876-10880. (1993)

藤木研究室

2012

Natsuyama, R., Okumoto, K., and Fujki, Y.: Peroxisome targeting signal type-1 receptor, Pex5p, stabilizes Pex14p: Study using a newly isolated pex5 CHO cell mutant, ZPEG101. Biochem. J. in press (2012).

Otera, H., and Fujiki, Y.: Pex5p imports folded terameric catalase by interaction with Pex13p. Traffic, 13: 1364-1377 (2012) .

Fujiki, Y., Yagita, Y., and Matsuzaki, T.: Peroxisome biogenesis disorders: molecular basis for impaired peoxisomal membrane assembly. Biochim. Biophys. Acta-Mol. Basis Dis. 1822: 1337-1342 (2012).

Umemoto., T., and fujiki, Y.: Ligand-dependent nucleo-cytoplasmic shuttling of peroxisome proliferators-activated receptors, PPARa and PPARg. Genes Cells, 17: 576-596 (2012).

Kanzawa, N., shimozawa, N., Wanders, R.J.A., Ikeda, K., Murakami, Y., Waterham, H.R., Mukai, S., Fujita, M., Maeda, Y., Taguchi, R., Fujiki, Y., and Kinoshita, T.: Defective lipid remodeling of GPI anchors in peroxisomal disorders, Zellweger syndrome and rhizomelic chondrodysplasia punctata. J.Lipid Res. 53: 653-663(2012).

Itoyama, A., Honsho, M., Abe, Y., Moser, A., Yoshida, Y., and Fujiki, Y.: Docosahexaenoic acid mediates peroxisomal elongation, a prerequisite for peroxisome division. J.Cell Sci. 125: 589-602 (2012).

Miyata, N., Okumoto, K., Noguchi, M., Mukai, S., and Fujiki, Y.: AWP1/ZFAND6 functions in Pex5 export by interacting with Cys-monoubiquitinated Pex5 and Pex6 AAA ATPase. Traffic 13: 168-183 (2012).

Fujiki, Y., Nashiro, C., Miyata, N., Tamura, S., Okumoto, K.: New insights into dynamic and funcional assembly of the AAA peroxins, Pex1p and Pex6p, and their membrane receptor Pex26p in shuttling of PTS1-receptor Pex5p during peroxisome biogenesis. Biochim. Biophys. Acta-Mol. Cell Biol. 1823:145-149 (2012).

2011

Miyata, N., Okumoto, K., Noguchi, M., Mukai, S., and Fujiki, Y.: AWP1/ZFAND6 functions in Pex5 export by interacting with Cys-monoubiquitinated Pex5 and Pex6 AAA ATPase. Traffic, in press.

Yonekawa, S., Furuno, A., Baba, T., Fujiki, Y., Ogasawara, Y., Yamamoto, A., Tagaya, M., and Tani, K.: Sec16B is involved in the endoplasmic reticulum export of the peroxisomal membrane biogenesis factor peroxin 16 (Pex16) in mammalian cells. Proc. Natl. Acad. Sci. USA, 108: 12746-12751 (2011).

Okumoto, K., Misono, S., Miyata, N., Matsumoto, Y., Mukai, S., and Fujiki, Y.: Cysteine-ubiquitination of peroxisome-targeting-signal type 1 (PTS1)-receptor Pex5p regulated Pex5p recycling. Traffic, 12: 1067-1083 (2011).

Nashiro, C., Kashiwagi, A., Matsuzaki, T., Tamura, S., and Fujiki, Y.: Recruiting mechanism of the AAA peroxins, Pex1p and Pex6p, to Pex26p on peroxisome membrane. Traffic, 12: 774-788 (2011).

Fujiki, Y.: Peroxisome biogenesis Disorders. In: Encyclopedia of the Life Sciences, pp. 1-9, John Wiley & Sons, Chichester, UK (2011).

Iwamoto, F., Umemoto, T., Motojima, K., and Fujiki, Y.: Nuclear transport of peroxisome-proliferator activated receptor a. J. Biochem.,149: 311-319 (2011).

Honsho, M., Hashiguchi, Y., Ghaedi, K., and Fujiki, Y.: Interaction defect of the medium isoform of PTS1-receptor Pex5p with PTS2-receptor Pex7p abrogates the PTS2 protein import into peroxisomes in mammals. J. Biochem., 149: 203-210 (2011).

2010

8) Yano, T., Oku, M., Akeyama, N., Itoyama, A., Yurimoto, H., Kuge, S., Fujiki, Y., and Sakai, Y.: A novel fluorescent sensor protein for visualization of redox states in the cytoplasm and in peroxisomes. Mol. Cell. Biol., 30: 3758-3766 (2010).

9) Su, J. R., Takeda, K., Tamura, S., Fujiki, Y., and Miki, T.: Monomer-dimer transition of the conserved N-terminal domain of the mammalian peroxisomal matrix protein import receptor, Pex14p. Biochem. Biophys. Res. Commun., 394: 217-221 (2010).

10) Honsho, M., Asaoku, S., and Fujiki, Y.: Posttranslational regulation of fatty acyl-CoA reductase 1, Far1, controls ether glycerophospholipid synthesis. J. Biol. Chem., 285: 8537-8542 (2010).

2009

11) Miyata,N., Hosoi, K., Mukai, S. and Fujiki, Y.: In vitro import of peroxisome-targeting signal type 2 (PTS2) receptor Pex7p into peroxisomes. Biochim. Biophys. Acta-Mol. Cell Res., 1793: 860-870 (2009).

12) Su, J. R., Takeda, K., Tamura, S., Fujiki, Y., and Miki, T.: Crystal structure of the conserved N-terminal domain of the peroxisomal matrix protein import receptor, Pex14p. Proc. Natl. Acad. Sci. USA, 106: 417-421 (2009).

2008

13) Matsuzaki, T., and Fujiki, Y.: The peroxisomal membrane-protein import receptor Pex3p is direcly transported to peroxisomes by a novel Pex19p- and Pex16p-dependent pathway. J. Cell Biol., 183: 1275-1286 (2008).

14) Chalupnikova, K., Lattmann, S., Selak, N., Iwamoto, F., Fujiki, Y., and Nagamine, Y.: Recruitment of the RNA helicase RHAU to stress granules via a unique RNA-binding domain. J. Biol. Chem., 283: 35186-35198 (2008).

15) Hara-Kuge, S., and Fujiki, Y.: The peroxin Pex14p is involved in LC3-dependent degradation of mammalian peroxisomes. Exp. Cell Res. , 314: 3531-3541 (2008).

16) Honsho, M., Yagita, Y., Kinoshita, N., and Fujiki, Y.: Isolation and characterization of mutant animal cell line defective in alkyl-dihydroxyacetonephosphate synthase: Localization and transport of plasmalogens to post-Golgi compartments. Biochim. Biophys. Acta.-Mol. Cell Res., 1783: 1857-1865 (2008).

17) Ghaedi, K., and Fujiki, Y.: Isolation and characterization of novel phenotype CHO cell mutants defective in peroxisome assembly, using ICR191 as a Potent mutagenic agent. Cell Biochem. Funct., 26: 684-691 (2008).

18) Sato, Y., Shibata, H., Nakano, H, Matsuzono, Y., Kashiwayama, Y., Kobayashi, Y., Fujiki, Y., Imanaka, T., and Kato, H.: Characterization of the interaction between recominant human peroxin PEX3p and PEX19p: Identification of TRP104 in Pex3p as a Critical residue for the interaction. J. Biol. Chem., 283: 6136-6144 (2008).

19) Fujiki, Y., Miyata, N., Matsumoto, N., and Tamura, S.: Dynamic and Functional assembly of the AAA peroxins, Pex1p and Pex6p, their membrane receptor Pex26p involved in shuttling of th PTS1 receptor Pex5p in peroxisome biogenesis. Biochem. Soc. Trans., 36: 109-113 (2008).

2007

20) Saito, M., Horikawa, M., Iwamori, Y., Sakakihara, Y., Mizuguchi, M., Igarashi, T., Fujiki, Y., and Iwamori, M.: Alterations in the molecular species of plasmalogen phospholipids and glycolipids due to peroxisomal dysfunction in Chinese hamster ovary-mutant Z65 cells by FABMS method. J. Chromatogr. B, 852: 367-373 (2007).

21) Kobayashi, S., Tanaka, A., and Fujiki, Y.: Fis1, DLP1, and Pex11p coordinately regulate peroxisome morphogenesis. Exp. Cell Res.,313: 1675-1686 (2007).

2006

22) Fujiki, Y,, Matsuzono, Y., and Matsuzaki, T.: Biogenesis of peroxisomal membranes: Pex3p-Pex19p system. Biochim. Biophys. Acta.-Mol. Cell Res., 1763: 1639-1646 (2006).

23) Fujiki, Y. Okumoto, K., Kinosita, N., and Ghaedi, K.: Model organisms in peroxisome biogenesis reseach: Lessons from peroxisome-deficient Chinese hamster ovary (CHO) cell mutants. Biochim. Biophys. Acta.-Mol. Cell Res., 1763: 1374-81 (2006).

24) Mukai, S., and Fujiki, Y.: Molecular mechanisms of import of peroxisome-targeting-signal type 2 (PTS2)-proteins by PTS2-receptor Pex7p and PTS1-receptor Pex5pL. J. Biol. Chem. 281:37311-37320 (2006).

25) Tamura, S., Yasutake, S., Matsumoto, N., and Fujiki, Y.: Dynamic and functional assembly of the AAA peroxins, Pex1p and Pex6p, and their membrane receptor Pex26p. J. Biol. Chem., 281: 27693-27704 (2006).

26) Matsuzono, Y., Matsuzaki, T., and Fujiki, Y.: Functional domain mapping of peroxin Pex19p: interaction with Pex3p is essential for function and translocation. J. Cell Sci., 119: 3539-3550 (2006).

27) Fan, W., and Fujiki, Y.: A temperature-sensitive CHO pex1 mutant with a novel mutation in the AAA Walker motif A1. Biochem. Biophys. Res. Commun. 345: 1434-1439 (2006).

28) Itoh, R., and Fujiki, Y.: Functional domains and dynamic assembly of the Peroxin Pex14p, the entry site of matrix proteins. J. Biol. Chem., 281: 10196-205 (2006).

29) Tanaka, A., Kobayashi, S., and Fujiki, Y.: Peroxisome division is impaired in a CHO cell mutant with an inactivating point-mutation in dynamin-like protein 1 gene. Exp. Cell Res., 312: 1671-84 (2006). *Adopted as ‘Highlight paper’

30) Furuki, S., Tamura, S., Matsumoto, N., Miyata, N., Moser, A., Moser, H.W., and Fujiki, Y.: Mutations in the peroxin Pex26p responsible for peroxisome biogenesis disorders of complementation group 8 impair its stability, peroxisomal localization, and interaction with Pex1p-Pex6p complex. J. Biol. Chem. 281: 1317-1323 (2006).

31) Matsuzono, Y., and Fujiki, Y.: In vitro transport of membrane proteins to peroxisomes by shuttling receptor Pex19p. J. Biol. Chem. 281: 36-42 (2006).

2005

32) Miyata, N., and Fujiki, Y.: Shuttling mechanism of peroxisome targeting signal type 1 receptor, Pex5p: ATP-independent import and ATP-dependent export. Mol. Cell. Biol. 25: 10822-10832 (2005).

2004

33) Ishizuka, M., Toyama, Y., Watanabe, H., Fujiki, Y., Takeuchi, A., Yamasaki, S., Yuasa, S., Miyazaki, M., Nakajima, N., Taki, S., and Saito, T.: Overexpression of human acyl-CoA thioesterase upregulates peroxisome biogenesis. Exp. Cell Res. 297: 127-141 (2004).

2003

34) Tanaka, A., Okumoto, K., and Fujiki, Y.: cDNA cloning and characterization of the third isoform of human peroxin Pex11p. Biochem. Biophys. Res. Commun. 300: 819-823 (2003).

35) Matsumoto, N., Tamura, S., and Fujiki, Y.: The pathogenic peroxin Pex26p recruits the Pex1p-Pex6p AAA-ATPase complexes to peroxisomes. Nat. Cell Biol. 5: 454-460 (2003).

36) Matsumoto, N., Tamura, S., Furuki, S., Miyata, N., Moser, A., Shimozawa, N., Moser, H.W., Suzuki, Y., Kondo, N., and Fujiki, Y.: Mutations in novel peroxin gene PEX26 that cause peroxisome biogenesis disorders of complementation group 8 provide a genotype-phenotype correlation. Am. J. Hum. Genet. 73: in press (2003) (published online on Juy 8, 2003).

37) Fujiki, Y.: Functional complementation. In: nature Encyclopedia of the Human Genome, Cooper, D.N. ed., vol. 2, pp. 539-543, Nature Publishing Group, London (2003).

38) Fujiki, Y.: Peroxisome biogenesis disorders. In: nature Encyclopedia of the Human Genome, Cooper, D.N. ed., vol. 4, pp. 541-547, Nature Publishing Group, London (2003).

2002

39) Mukai, S., Ghaedi, K., and Fujiki, Y.: Intracellular localization, function, and dysfunction of the peroxisome-targeting signal type 2 receptor, Pex7p, in mammalian cells. J. Biol. Chem. 277: 9548-9561 (2002).

40) Otera, H., Setoguchi, K., Hamasaki, M., Kumashiro, T., Shimizu, N., and Fujiki, Y.: Peroxisomal targeting signal receptor Pex5p interacts with cargoes and import machinery components in a spatiotemporally differentiated manner: conserved Pex5p WXXXF/Y motifs are critical for matrix protein import. Mol. Cell. Biol. 22: 1639-1655 (2002).

41) Shimozawa, N., Nagase, T., Takemoto, Y., Suzuki, Y., Fujiki, Y., Wanders, R.J.A.. and Kondo, N.: A novel aberrant splicing mutation of the PEX16 gene in two patients with Zellweger syndrome. Biochem. Biophys. Res. Commun. 292: 109-112 (2002).

42) Yanago, E., Hiromasa, T., Matsumura, T., Kinoshita, N., and Fujiki, Y.: Isolation of Chinese hamster ovary cell pex mutants: two PEX7-defective mutants. Biochem. Biophys. Res. Commun. 293: 225-230 (2002).

43) Akiyama, N., Ghaedi, K., and Fujiki, Y.: A novel pex2 mutant: catalase-deficient but temperature-sensitive PTS1 and PTS2 import. Biochem. Biophys. Res. Commun. 293: 1523-1529 (2002).

44) Saito, M., Fukushima, Y., Tatsumi, K., Bei, L., Fujiki, Y., Iwamori, M., Igarashi, T., and Sakakihara, Y.: Molecular cloning of Chinese hamster ceramide glucosyltransferase and its enhanced expression in peroxisome-defective mutant Z65 cells. Arch. Biochem. Biophys. 403: 171-178 (2002).

45) Honsho, M., Hiroshige, T., and Fujiki, Y.: The membrane biogenesis peroxin Pex16p: topogenesis and functional roles in peroxisomal membrane assembly. J. Biol. Chem. 277: 44513-44524 (2002).

46) Fujiki, Y. Peroxisome assembly and peroxisome biogenesis disorders. In: Genome Science – Towards a New Paradaigm? (International Congress Series 1246) (H. Yoshikawa, N. Ogasawara, and N. Satoh, eds) pp 33-42 (Elsevier Science Amsterdam) (2002).

2001

47) Otera, H., Nishimura, M., Setoguchi, K., Mori, T., and Fujiki, Y.: Biogenesis of nonspecific lipid transfer protein and sterol carrier protein x: STUDIES USING PEROXISOME ASSEMBLY-DEFECTIVE pex CELL MUTANTS. J. Biol. Chem. 276: 2858-2864 (2001).

48) Honsho, M., and Fujiki, Y.: Topogenesis of peroxisomal membrane protein requires a short, positively charged intervening-loop sequence and flanking hydrophobic segments: STUDY USING HUMAN MEMBRANE PROTEIN PMP34. J. Biol. Chem. 276: 9375-9382 (2001).

49) Matsumoto, N., Tamura, S., Moser, A., Moser, H.W., Braverman, N., Suzuki, Y., Shimozawa, N., Kondo, N., and Fujiki, Y.: The Peroxin Pex6p gene is impaired in peroxisome biogenesis disorders of complementation group 6. J. Hum. Genet. 46: 273-277 (2001).

50) Harano, T., Nose, S., Uezu, R., Shimizu, N., and Fujiki, Y.: Hsp70 regulates interaction of theperoxisome targeting signal type 1 (PTS1)-receptor Pex5p and PTS1. Biochem. J. 357: 157-165(2001).

51) Tamura, S., Matsumoto, N., Imamura, A., Shimozawa, N., Suzuki, Y., Kondo, N., and Fujiki, Y.: Phenotype-genotype relationships in peroxisome biogenesis disorders of PEX1-defective complementation group 1 are defined by Pex1p-Pex6p interaction. Biochem. J. 357: 417-426(2001).

52) Suzuki, Y., Shimozawa, N., Orii, T., Tsukamoto, T., Osumi, T., Fujiki, Y., and Kondo, N.: Genetic and molecular bases of peroxisome biogenesis disorders. Genet. Med. 3: 372-376 (2001).

2000

53) Fujiki, Y., Okumoto, K., Otera, H., and Tamura, S.: Peroxisome biogenesis and molecular defects in peroxisome assembly disorders. Cell Biochem. Biophys. 32: 155-164 (2000).

54) Otera, H., Harano, H., Honsho, M., Tanaka, A., Kawai, A., Shimizu, N., and Fujiki, Y.: Pex5pL, the longer isoform of mobile PTS1-receptor, functions in a novel and pivotal, Pex7p-mediated PTS2 import pathway via its initial docking site Pex14p. J. Biol. Chem. 275: 21703-21714 (2000).

55) Matsumura, T., Otera, H., and Fujiki, Y.: Disruption of interaction of the longer iso form of Pex5p, Pex5pL, with Pex7p abolishes the PTS2 protein import in mammals. Study with a novel PEX5-impaired Chinese hamster ovary cell mutant. J. Biol. Chem. 275: 21715-21721 (2000).

56) Ghaedi, K., Tamura, S., Okumoto, K., Matsuzono, Y., and Fujiki, Y.: The peroxin Pex3p initiates membrane assembly in peroxisome biogenesis. Mol. Biol. Cell 11: 2085-2102 (2000).

57) Okumoto, K., Abe, I., and Fujiki, Y.: Molecular anatomy of the Peroxin Pex12p: RING finger domain is essential for the Pex12p function and interacts with the peroxisome targeting signal type1-receptor Pex5p and a RING peroxin, Pex10p. J. Biol. Chem. 275: 25700-25710 (2000).

58) Fujiki, Y.: Review: Peroxisome biogenesis and peroxisome biogenesis disorders. FEBS Lett. 476,42-46 (2000).

59) Ghaedi, K., Honsho, M., Shimozawa, N., Suzuki, Y., Kondo, N., and Fujiki, Y.: PEX3 is the causal gene responsible for peroxisome membrane assembly-defective Zellweger syndrome of complementation group G. Am. J. Hum. Genet. 67: 976-981 (2000).

1999

60) Matsuzono, Y., Kinoshita, N., Tamura, S., Shimozawa, N., Hamasaki, M., Ghaedi, K., Wanders, R. J. A., Suzuki, Y., Kondo, N., and Fujiki, Y.: Human PEX19: cDNA cloning by functional complementation, mutation analysis in a patient with Zellweger syndrome and potential role in peroxisomal membrane assembly. Proc. Natl. Acad. Sci. USA. 96: 2116-2121 (1999).

61) Shimizu, N., Itoh, R., Hirono, H., Otera, H., Ghaedi, K., Tateishi, K., Tamura, S., Okumoto, K., Harano, T., Mukai, S., and Fujiki, Y.: The Peroxin Pex14p: cDNA cloning by functional complementation on a Chinese hamster ovary cell mutant, characterization, and functional analysis. J. Biol. Chem. 274: 12593-12604 (1999).

62) Ghaedi, K., Itagaki, A., Toyama, R., Tamura, S., Matsumura, T., Kawai, A., Shimozawa, N., Suzuki, Y., Kondo, N., and Fujiki, Y.: Newly identified Chinese hamster ovary cell mutants defective in peroxisome assembly represent complementation group A of human peroxisome biogenesis disorders and one novel group in mammals. Exp. Cell Res. 248: 482-488 (1999).

63) Ghaedi, K., Kawai, A., Okumoto, K., Tamura, S., Shimozawa, N., Suzuki, Y., Kondo, N., and Fujiki, Y.: Isolation and characterization of novel peroxisome biogenesis-defective Chinese hamster ovary cell mutants using green fluorescent protein. Exp. Cell Res. 248: 489-497 (1999).

64) Harano, T., Shimizu, N., Otera, H., and Fujiki, Y.: Transmembrane topology of the peroxin Pex2p, an essential component of peroxisome assembly. J. Biochem. 125: 1168-1174 (1999).

65) Toyama, R., Mukai, S., Itagaki, A., Tamura, S., Shimozawa, N., Suzuki, Y., Kondo, N., Wanders, R.J.A., and Fujiki, Y.: Isolation, characterization, and mutation analysis of PEX13-defective Chinese hamster ovary cell mutants. Hum. Mol. Genet. 8: 1673-1681 (1999).

1998

66) Otera, T., Okumoto, K., Tateishi, K., Ikoma, Y., Matsuda, E., Nishimura, M., Tsukamoto, T., Osumi, T., Ohashi, K., Higuchi, O., and Fujiki, Y.: Peroxisome targeting signal type 1 (PTS1)- receptor is involved in import of both PTS1 and PTS2: Studies with PEX5-defective CHO cell mutants. Mol. Cell. Biol. 18: 388-399 (1998).

67) Tamura, S., Okumoto, K., Toyama, R., Shimozawa, N., Tsukamoto, T., Suzuki, Y., Osumi, T., Kondo, N., and Fujiki, Y.: Human PEX1 cloned by functional complementation on a CHO cell mutant is responsible for peroxisome-deficient Zellweger syndrome of complementation group I. Proc. Natl. Acad. Sci. USA 95: 4350-4355 (1998).

68) Tamura, S., Shimozawa, N., Suzuki, Y., Tsukamoto, T., Osumi, T., and Fujiki, Y.: A cytoplasmic AAA family peroxin, Pex1p, interacts with Pex6p. Biochem. Biophys. Res. Commun. 245: 883-886 (1998).

69) Okumoto, K., Shimozawa, N., Kawai, A., Tamura, S., Tsukamoto, T., Osumi, T., Moser, H., Wanders, R.J.A., Suzuki, Y., Kondo, N., and Fujiki, Y.: PEX12, the pathogenic gene of group III Zellweger syndrome: cDNA cloning by functional complementation on a CHO cell mutant, patient analysis, and characterization of Pex12p. Mol. Cell. Biol. 18: 4324-4336 (1998).

70) Kinoshita, N., Ghaedi, K., Shimozawa, N., Wanders, R. J. A., Matsuzono, Y., Imanaka, T., Okumoto, K., Suzuki, Y., Kondo, N., and Fujiki, Y.: Newly identified Chinese hamster ovary cell mutants are defective in biogenesis of peroxisomal membrane vesicles (peroxisomal ghosts), representing a novel complementation group in mammals. J. Biol. Chem. 273: 24122-24130 (1998).

71) Okumoto, K., Itoh, R., Shimozawa, N., Suzuki, Y., Tamura, S., Kondo, N., and Fujiki, Y.: Mutation in PEX10 is the cause of Zellweger peroxisome-deficiency syndrome of complementation group B. Hum. Mol. Genet. 7: 1399-1405 (1998).

72) Abe, I., Okumoto, K., Tamura, S., and Fujiki, Y.: Clofibrate-inducible, 28-kDa peroxisomal integral membrane protein is encoded by PEX11. FEBS Lett. 431: 468-472 (1998).

73) Abe, I., and Fujiki, Y.: cDNA cloning and characterization of a constitutively expressed isoform of the human peroxin Pex11p. Biochem. Biophys. Res. Commun. 252: 529-533 (1998).

74) Imamura, A., Tamura, S., Shimozawa, N., Suzuki, Y., Zhang, Z., Tsukamoto, T., Orii, T., Kondo, N., Osumi, T., and Fujiki, Y.: Temperature-sensitive mutation in PEX1 moderates the phenotypes of peroxisome deficiency disorders. Hum. Mol. Genet. 7: 2089-2094 (1998).

75) Honsho, M., Tamura, S., Shimozawa, N., Suzuki, Y., Kondo, N., and Fujiki, Y.: Mutation in PEX16 is causal in the peroxisome-deficient Zellweger syndrome of complementation group D. Am. J. Hum. Genet. 63: 1622-1630 (1998).

76) Shimozawa, N., Suzuki, Y., Zhang, Z., Imamura, A., Kondo, N., Kinoshita, N., Fujiki, Y., Tsukamoto, T., Osumi, T., Imanaka, T., Orii, T., Beemer, F., Mooijer, P., Dekker, C., and Wanders, R.J.A.: Genetic basis of peroxisome assembly mutants of humans, CHO cells and yeast: identification of a new complementation group of peroxisome biogenesis disorders, absent from peroxisomal membrane ghosts. Am. J. Hum. Genet. 63: 1898-1902 (1998).

1997

77) Fujiki, Y.: Peroxisome biogenesis and peroxisome assembly disorders. In Membrane Proteins: Structure, Function and Expression Control (Mihara, K. and Hamasaki, N. eds.), Karger Press, Basel, pp.53-61 (1997) .

78) Okumoto, K., Bogaki, A., TateishiI, K., Tsukamoto, T., Osumi, T., Shimozawa, N., Suzuki, Y., Orii, T., and Fujiki, Y.: Isolation and characterization of peroxisome-deficient Chinese hamster ovary (CHO) cell mutants representing human complementation group III. Exp. Cell Res. 233: 11-20 (1997).

79) Tateishi, K., Okumoto, K., Shimozawa, N., Tsukamoto, T., Osumi, T., Suzuki, Y., Kondo, N., Okano, I., and Fujiki, Y.: Newly identified CHO cell mutants defective in peroxisome biogenesis represent two novel complementation groups in mammals. Eur. J. Cell Biol. 73: 352-359 (1997).

80) Fujiki, Y.: Review: Molecular defects in genetic diseases of peroxisomes. Biochim. Biophys. Acta 1361: 235-250 (1997).

81) Okumoto, K., and Fujiki, Y.:PEX12 encodes an integral membrane protein of peroxisomes. Nature Genet. 17: 265-266 (1997).

1996

82) Fujiki, Y.: Peroxisome biogenesis: topogenic signal, peroxisome assembly factor, and Zellweger syndrome. In Membrane Protein Transport (S. Rothman, ed.), Advances in Molecular and Cell Biology: Membrane Protein Transport, Vol. 3, pp. 213-229 (1996).

83) Distel, B., Erdmann, R., Gould, S.J., Blobel, G., Crane, D.I., Cregg, J.M., Dodt, G., Fujiki, Y., et al.: A unified nomenclature for peroxisome biogenesis factors. J. Cell Biol. 135:1-3 (1996).

84) Fujiki, Y.: Approaches to studies on peroxisome biogenesis and human peroxisome-deficient disorders. Ann. N. Y. Acad. Sci. 804: 491-501 (1996).

邦文総説

1) 藤木幸夫、奥本寛治:ペルオキシソームの形成とその異常症. 蛋白質・核酸・酵素, 45: 691-699 (2000).

2) 藤木幸夫:Peroxisome deficiency の分子機構. 遺伝子医学 4: 306-312 (2000).

3) 藤木幸夫 :ペルオキシソーム—- オルガネラ界の新スターは異端児か? 「バイオサイエンスの新世 紀」(日本生化学会)第2巻「タンパク質の一生:タンパク質の誕生・成熟から死まで」中野明彦・遠藤斗志也(編)、共立出版、東京、pp. 137-152 (2000).

4) 藤木幸夫:ペルオキシソームの形成とペルオキシソーム病. 特集「細胞内蛋白質輸送のダイナミクス」 細胞 33: 177-180 (2001).

5) 藤木幸夫、大寺秀典、ガエディ・カムラン:ペルオキシソーム形成の分子機構と障害. 「特集 細胞内タンパク質輸送:細胞質・オルガネラを結ぶネットワーク」実験医学 20: 987-992 (2002).

6) 藤木幸夫:ペルオキシソームの形成. わかる実験医学シリーズ「細胞内輸送がわかる」米田悦啓(編)羊土社、 pp. 61-67 (2002).

7) 藤木幸夫:ペルオキシソームの形成制御と病態. 特集「細胞機能の調節:タンパク質の細胞内トラフィックとオルガネラの形成と制御」 生化学 75(6): 459-654 (2003).

8) 藤木幸夫:ペルオキシソーム欠損症病因遺伝子PEX26. 医学のあゆみ, 206: 922-923 (2003).

9) 藤木幸夫:ペルオキシソームの形成機構とペルオキシソーム病. 蛋白質・核酸・酵素 増刊号「細胞における蛋白質の一生」, 49: 1136-114 (2004).

10) 藤木幸夫:ペルオキシソームの形成・分裂形態制御およびその障害の分子基盤. 日本応用酵素協会誌, 42: 23-24 (2007).

11) 藤木幸夫:ペルオキシソームの形成機構とその破綻. 膜, 33: 9-16 (2008).

12) 藤木幸夫:Zellweger症候群. 小児科診療2009年増刊号, 72: 364-5 (2009).

13) 藤木幸夫、宮田暖、松園裕嗣、松崎高志、本庄雅則:ペルオキシソームの形成・制御とその障害による高次機能の破綻. 「特集 Protein Kinesisを解き明かすオルガネラの世界 細胞機能の制御と遺伝病発症・ウイルス感染のメカニズム」実験医学 28: 2094-2101 (2010).