Journal ArticleDOI
Glycosylphosphatidylinositol mannosyltransferase II is the rate-limiting enzyme in glycosylphosphatidylinositol biosynthesis under limited dolichol-phosphate mannose availability
Tetsuya Hirata,Morihisa Fujita,Noriyuki Kanzawa,Yoshiko Murakami,Yusuke Maeda,Taroh Kinoshita +5 more
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TLDR
Overexpression of PIGV, which encodes GPI mannosyltransferase II, restored the surface expression of CD59 and normalized the accumulation of GPI intermediates in the mutant cells, suggesting that GPIMannosyl transferase II is the rate-limiting enzyme in GPI biosynthesis under limited dolichol-phosphate mannose availability.Abstract:
Although the genes involved in the biosynthesis of glycosylphosphatidylinositol (GPI) are well characterized, the regulation of GPI biosynthesis remains unclear. We isolated and characterized a mutant cell line showing decreased surface expression of CD59 and the accumulation of GPI intermediates. The mutant cell line was partially defective in MPDU1, which encodes a protein required for the utilization of dolichol-phosphate mannose. Overexpression of PIGV, which encodes GPI mannosyltransferase II, restored the surface expression of CD59 and normalized the accumulation of GPI intermediates in the mutant cells. Among all known genes involved in GPI biosynthetic pathway, only PIGV had such suppressive activity. PIGV, however, did not restore the abnormality of N-glycosylation caused by MPDU1 mutation. Our results suggest that GPI mannosyltransferase II is the rate-limiting enzyme in GPI biosynthesis under limited dolichol-phosphate mannose availability.read more
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Post-Golgi anterograde transport requires GARP-dependent endosome-to-TGN retrograde transport
Tetsuya Hirata,Morihisa Fujita,Shota Nakamura,Kazuyoshi Gotoh,Daisuke Motooka,Yoshiko Murakami,Yusuke Maeda,Taroh Kinoshita +7 more
TL;DR: GARP (tethering factor)- and VAMP4 (v-SNARE)-dependent endosome-to-TGN retrograde transport is required for the efficient post-Golgi anterograde transport of cell-surface integral membrane proteins.
Journal ArticleDOI
Quantitative, Time-Resolved Proteomic Analysis by Combining Bioorthogonal Noncanonical Amino Acid Tagging and Pulsed Stable Isotope Labeling by Amino Acids in Cell Culture
John D. Bagert,Yushu J. Xie,Michael J. Sweredoski,Yutao Qi,Sonja Hess,Erin M. Schuman,David A. Tirrell +6 more
TL;DR: An approach to proteomic analysis that combines bioorthogonal noncanonical amino acid tagging (BONCAT) and pulsed stable isotope labeling with amino acids in cell culture (pSILAC) provides accurate quantitative information about rates of cellular protein synthesis on time scales of minutes.
Journal ArticleDOI
N-Glycan-dependent protein folding and endoplasmic reticulum retention regulate GPI-anchor processing.
Yi-Shi Liu,Xin-Yu Guo,Tetsuya Hirata,Yao Rong,Daisuke Motooka,Toshihiko Kitajima,Yoshiko Murakami,Xiao-Dong Gao,Shota Nakamura,Taroh Kinoshita,Morihisa Fujita +10 more
TL;DR: Results indicated that N-glycans participate in quality control and temporal ER retention of GPI-APs, ensuring their correct folding and GPI processing before exiting from the ER.
Journal ArticleDOI
Skin manifestations in CDG
Daisy Rymen,Jaak Jaeken +1 more
TL;DR: The variety of skin manifestations reported in CDG is discussed and the possible mechanisms that link a certain glycosylation deficiency to its skin phenotype are explored.
Journal ArticleDOI
Identification of a Golgi GPI-N-acetylgalactosamine transferase with tandem transmembrane regions in the catalytic domain.
Tetsuya Hirata,Sushil Kumar Mishra,Shota Nakamura,Kazunobu Saito,Daisuke Motooka,Yoko Takada,Noriyuki Kanzawa,Yoshiko Murakami,Yusuke Maeda,Morihisa Fujita,Yoshiki Yamaguchi,Taroh Kinoshita +11 more
TL;DR: It is suggested that a juxtamembrane region of PGAP4 accommodates various GPI-anchored proteins, presenting their acceptor residue toward the catalytic center, and elucidate the initial step of G PI-GalNAc biosynthesis.
References
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Journal ArticleDOI
Deficiency of Dol-P-Man synthase subunit DPM3 bridges the congenital disorders of glycosylation with the dystroglycanopathies.
Dirk J. Lefeber,Johannes Schönberger,Eva Morava,Maïlys Guillard,Karin M Huyben,Kiek Verrijp,Olga Grafakou,Athanasios Evangeliou,Frank Preijers,Panagiota Manta,Jef Yildiz,Stephanie Grunewald,Martha Spilioti,Christa van den Elzen,Dominique Klein,Daniel Hess,Hisashi Ashida,Jan Hofsteenge,Yusuke Maeda,Lambertus P. van den Heuvel,Martin Lammens,Ludwig Lehle,Ron A. Wevers +22 more
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Journal ArticleDOI
Fatty Acid Remodeling of GPI-anchored Proteins Is Required for Their Raft Association
Yusuke Maeda,Yuko Tashima,Toshiaki Houjou,Morihisa Fujita,Takehiko Yoko-o,Yoshifumi Jigami,Ryo Taguchi,Taroh Kinoshita +7 more
TL;DR: It is reported that GPI-APs, with two saturated fatty chains, are generated from those bearing an unsaturated chain by fatty acid remodeling that occurs most likely in the Golgi and requires post-GPI-attachment to proteins (PGAP)2 and PGAP3 and shows that the remodeling requires the preceding PGAP1-mediated deacylation from inositol of GPI -APs in the endoplasmic reticulum.