九州大学 研究者情報
論文一覧
宮田 暖(みやた のん) データ更新日:2022.06.14

助教 /  理学研究院 化学部門 有機・生物化学講座


原著論文
1. 宮田 暖,伊藤 貴紀,中島 美由,藤井 悟,久下 理, Mitochondrial phosphatidylethanolamine synthesis affects mitochondrial energy metabolism and quiescence entry through attenuation of Snf1/AMPK signaling in yeast., FASEB Journal, 10.1096/fj.202101600RR, 36, 7, e22355, 2022.07.
2. 宮田 暖,久下 理, Topology of phosphatidylserine synthase 1 in the endoplasmic reticulum membrane, PROTEIN SCIENCE, 10.1002/pro.4182, 30, 11, 2346-2353, 2021.11.
3. Sakaue, Haruka; Shiota, Takuya; Ishizaka, Naoya; Kawano, Shin; Tamura, Yasushi; Tan, Kher Shing; Imai, Kenichiro; Motono, Chie; Hirokawa, Takatsugu; Taki, Kentaro; Miyata, Non; Kuge, Osamu; Lithgow, Trevor; Endo, Toshiya, Porin Associates with Tom22 to Regulate the Mitochondrial Protein Gate Assembly, MOLECULAR CELL, 10.1016/j.molcel.2019.01.003, 73, 5, 1044-+, 2019.03.
4. Non Miyata, Satoru Fujii, Osamu Kuge, Porin proteins have critical functions in mitochondrial phospholipid metabolism in yeast, The Journal of Biological Chemistry, DOI 10.1074/jbc.RA118.005410, 293, 45, 17593-17605, 2018.11.
5. Non Miyata, Naoto Goda, Keiji Matsuo, Takeshi Hoketsu, Osamu Kuge, Cooperative function of Fmp30, Mdm31, and Mdm32 in Ups1-independent cardiolipin accumulation in the yeast Saccharomyces cerevisiae, Scientific Reports, 10.1038/s41598-017-16661-2, 7, 1, 2017.12.
6. Hosoi KI, Miyata N, Mukai S, Furuki S, Okumoto K, Cheng EH, Fujiki Y, The VDAC2-BAK axis regulates peroxisomal membrane permeability., The Journal of Cell Biology, 10.1083/jcb.201605002, 216, 3, 709-722, 2017.03, Peroxisomal biogenesis disorders (PBDs) are fatal genetic diseases consisting of 14 complementation groups (CGs). We previously isolated a peroxisome-deficient Chinese hamster ovary cell mutant, ZP114, which belongs to none of these CGs. Using a functional screening strategy, VDAC2 was identified as rescuing the peroxisomal deficiency of ZP114 where VDAC2 expression was not detected. Interestingly, knockdown of BAK or overexpression of the BAK inhibitors BCL-XL and MCL-1 restored peroxisomal biogenesis in ZP114 cells. Although VDAC2 is not localized to the peroxisome, loss of VDAC2 shifts the localization of BAK from mitochondria to peroxisomes, resulting in peroxisomal deficiency. Introduction of peroxisome-targeted BAK harboring the Pex26p transmembrane region into wild-type cells resulted in the release of peroxisomal matrix proteins to cytosol. Moreover, overexpression of BAK activators PUMA and BIM permeabilized peroxisomes in a BAK-dependent manner. Collectively, these findings suggest that BAK plays a role in peroxisomal permeability, similar to mitochondrial outer membrane permeabilization..
7. Miyata N, Tang Z, Conti MA, Johnson ME, Douglas CJ, Hasson SA, Damoiseaux R, Chang CA, Koehler CM, Adaptation of a Genetic Screen Reveals an Inhibitor for Mitochondrial Protein Import Component Tim44., The Journal of Biological Chemistry, 10.1074/jbc.M116.770131, 292, 13, 5429-5442, 2017.03, Diverse protein import pathways into mitochondria use translocons on the outer membrane (TOM) and inner membrane (TIM). We adapted a genetic screen, based on Ura3 mistargeting from mitochondria to the cytosol, to identify small molecules that attenuated protein import. Small molecule mitochondrial import blockers of the Carla Koehler laboratory (MB)-10 inhibited import of substrates that require the TIM23 translocon. Mutational analysis coupled with molecular docking and molecular dynamics modeling revealed that MB-10 binds to a specific pocket in the C-terminal domain of Tim44 of the protein-associated motor (PAM) complex. This region was proposed to anchor Tim44 to the membrane, but biochemical studies with MB-10 show that this region is required for binding to the translocating precursor and binding to mtHsp70 in low ATP conditions. This study also supports a direct role for the PAM complex in the import of substrates that are laterally sorted to the inner membrane, as well as the mitochondrial matrix. Thus, MB-10 is the first small molecule modulator to attenuate PAM complex activity, likely through binding to the C-terminal region of Tim44..
8. Miyata N, Watanabe Y, Tamura Y, Endo T, Kuge O, Phosphatidylserine transport by Ups2-Mdm35 in respiration-active mitochondria, The Journal of Cell Biology, 10.1083/jcb.201601082, 214, 1, 77-88, 2016.07, Phosphatidylethanolamine (PE) is an essential phospholipid for mitochondrial functions and is synthesized mainly by phosphatidylserine (PS) decarboxylase at the mitochondrial inner membrane. In Saccharomyces cerevisiae, PS is synthesized in the endoplasmic reticulum (ER), such that mitochondrial PE synthesis requires PS transport from the ER to the mitochondrial inner membrane. Here, we provide evidence that Ups2-Mdm35, a protein complex localized at the mitochondrial intermembrane space, mediates PS transport for PE synthesis in respiration-active mitochondria. UPS2- and MDM35-null mutations greatly attenuated conversion of PS to PE in yeast cells growing logarithmically under nonfermentable conditions, but not fermentable conditions. A recombinant Ups2-Mdm35 fusion protein exhibited phospholipid-transfer activity between liposomes in vitro. Furthermore, UPS2 expression was elevated under nonfermentable conditions and at the diauxic shift, the metabolic transition from glycolysis to oxidative phosphorylation. These results demonstrate that Ups2-Mdm35 functions as a PS transfer protein and enhances mitochondrial PE synthesis in response to the cellular metabolic state..
9. Otera H, Miyata N, Kuge O, Mihara K, Drp1-dependent mitochondrial fission via MiD49/51 is essential for apoptotic cristae remodeling., The Journal of Cell Biology, 10.1083/jcb.201508099, 12, 5, 531-544, 2016.02.
10. Miyata N, Miyoshi T, Yamaguchi T, Nakazono T, Tani M, Kuge O, Vid22 is required for transcriptional activation of the PSD2 gene in the yeast Saccharomyces cerevisiae., Biochemical Journal, 10.1042/BJ20150884, 472, 3, 319-328, 2015.12.
11. Miyata N, Steffen J, Johnson ME, Fargue S, Danpure CJ, Koehler CM, Pharmacologic rescue of an enzyme-trafficking defect in primary hyperoxaluria 1., Proceedings of the National Academy of Sciences of the United States of America, 10.1073/pnas.1408401111, 111, 40, 14406-14411, 2014.10, Primary hyperoxaluria 1 (PH1; Online Mendelian Inheritance in Man no. 259900), a typically lethal biochemical disorder, may be caused by the AGT(P11LG170R) allele in which the alanine:glyoxylate aminotransferase (AGT) enzyme is mistargeted from peroxisomes to mitochondria. AGT contains a C-terminal peroxisomal targeting sequence, but mutations generate an N-terminal mitochondrial targeting sequence that directs AGT from peroxisomes to mitochondria. Although AGT(P11LG170R) is functional, the enzyme must be in the peroxisome to detoxify glyoxylate by conversion to alanine; in disease, amassed glyoxylate in the peroxisome is transported to the cytosol and converted to oxalate by lactate dehydrogenase, leading to kidney failure. From a chemical genetic screen, we have identified small molecules that inhibit mitochondrial protein import. We tested whether one promising candidate, Food and Drug Administration (FDA)-approved dequalinium chloride (DECA), could restore proper peroxisomal trafficking of AGT(P11LG170R). Indeed, treatment with DECA inhibited AGT(P11LG170R) translocation into mitochondria and subsequently restored trafficking to peroxisomes. Previous studies have suggested that a mitochondrial uncoupler might work in a similar manner. Although the uncoupler carbonyl cyanide m-chlorophenyl hydrazone inhibited AGT(P11LG170R) import into mitochondria, AGT(P11LG170R) aggregated in the cytosol, and cells subsequently died. In a cellular model system that recapitulated oxalate accumulation, exposure to DECA reduced oxalate accumulation, similar to pyridoxine treatment that works in a small subset of PH1 patients. Moreover, treatment with both DECA and pyridoxine was additive in reducing oxalate levels. Thus, repurposing the FDA-approved DECA may be a pharmacologic strategy to treat PH1 patients with mutations in AGT because an additional 75 missense mutations in AGT may also result in mistrafficking..
12. Yien YY, Robledo RF, Schultz IJ, Takahashi-Makise N, Gwynn B, Bauer DE, Dass A, Yi G, Li L, Hildick-Smith GJ, Cooney JD, Pierce EL, Mohler K, Dailey TA, Miyata N, Paw BH, TMEM14C is required for erythroid mitochondrial heme metabolism., Journal of Clinical Investigation, 10.1172/JCI76979, 124, 10, 4294-4304, 2014.08.
13. Hildick-Smith GJ, Cooney JD, Garone C, Kremer LS, Tobias B, Thon JN, Miyata N, Paw BH, Macrocytic Anemia and Mitochondriopathy Resulting from a Defect in Sideroflexin 4, AMERICAN JOURNAL OF HUMAN GENETICS, 10.1016/j.ajhg.2013.09.011, 93, 5, 906-914, 2013.11.
14. Miyata N, Okumoto K, Mukai S, Noguchi M, Fujiki Y, AWP1/ZFAND6 Functions in Pex5 Export by Interacting with Cys-Monoubiquitinated Pex5 and Pex6 AAA ATPase, TRAFFIC, 10.1111/j.1600-0854.2011.01298.x, 13, 1, 168-183, 2012.01.
15. Fujiki Y, Nashiro C, Miyata N, Tamura S, 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, BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, 10.1016/j.bbamcr.2011.10.012, 1823, 1, 145-149, 2012.01.
16. Okumoto K, Misono S, Miyata N, Matsumoto Y, Mukai S, Fujiki Y, Cysteine Ubiquitination of PTS1 Receptor Pex5p Regulates Pex5p Recycling, TRAFFIC, 10.1111/j.1600-0854.2011.01217.x, 12, 8, 1067-1083, 2011.08.
17. Miyata N, Hosoi K, Mukai S, Fujiki Y, In vitro import of peroxisome-targeting signal type 2 (PTS2) receptor Pex7p into peroxisomes, BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, 10.1016/j.bbamcr.2009.02.007, 1793, 5, 860-870, 2009.05.
18. Briggs L, Baldwin G, Miyata N, Kondo H, Zhang X, Freemont PS, Analysis of nucleotide binding to p97 reveals the properties of a tandem AAA hexameric ATPase, JOURNAL OF BIOLOGICAL CHEMISTRY, 10.1074/jbc.M709632200, 283, 20, 13745-13752, 2008.05.
19. Fujiki Y, Miyata N, Matsumoto N, Tamura S, Dynamic and functional assembly of the AAA peroxins,, Pex1p and Pex6p, and their membrane receptor Pex26p involved in shuttling of the PTS1 receptor Pex5p in peroxisome biogenesis, BIOCHEMICAL SOCIETY TRANSACTIONS, 10.1042/BST0360109, 36, 109-113, 2008.02.
20. Miyata N, Fujiki Y, Shuttling mechanism of peroxisome targeting signal type 1 receptor Pex5: ATP-independent import and ATP-dependent export., Molecular and Cellular Biology, 10.1128/MCB.25.24.10822-10832.2005, 25, 24, 10822-10832, 2005.12.

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