Characterization of galactosyltransferase and sialyltransferase genes mediating the elongation of the extracellular O-GlcNAc glycans
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Characterization of galactosyltransferase and sialyltransferase genes mediating the elongation of the extracellular O-GlcNAc glycans. / Tsukamoto, Yohei; Tsukamoto, Natsumi; Saiki, Wataru; Tashima, Yuko; Furukawa, Jun ichi; Kizuka, Yasuhiko; Narimatsu, Yoshiki; Clausen, Henrik; Takeuchi, Hideyuki; Okajima, Tetsuya.
In: Biochemical and Biophysical Research Communications, Vol. 703, 149610, 2024.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Characterization of galactosyltransferase and sialyltransferase genes mediating the elongation of the extracellular O-GlcNAc glycans
AU - Tsukamoto, Yohei
AU - Tsukamoto, Natsumi
AU - Saiki, Wataru
AU - Tashima, Yuko
AU - Furukawa, Jun ichi
AU - Kizuka, Yasuhiko
AU - Narimatsu, Yoshiki
AU - Clausen, Henrik
AU - Takeuchi, Hideyuki
AU - Okajima, Tetsuya
N1 - Publisher Copyright: © 2024 Elsevier Inc.
PY - 2024
Y1 - 2024
N2 - O-GlcNAc is a unique post-translational modification found in cytoplasmic, nuclear, and mitochondrial proteins. In a limited number of extracellular proteins, O-GlcNAc modifications occur through the action of EOGT, which specifically modifies subsets of epidermal growth factor-like (EGF) domain-containing proteins such as Notch receptors. The abnormalities due to EOGT mutations in mice and humans and the increased EOGT expression in several cancers signify the importance of EOGT pathophysiology and extracellular O-GlcNAc. Unlike intracellular O-GlcNAc monosaccharides, extracellular O-GlcNAc extends to form elongated glycan structures. However, the enzymes involved in the O-GlcNAc glycan extension have not yet been reported. In our study, we comprehensively screened potential galactosyltransferase and sialyltransferase genes related to the canonical O-GlcNAc glycan pathway and revealed the essential roles of B4GALT1 and ST3GAL4 in O-GlcNAc glycan elongation in human HEK293 cells. These findings were confirmed by sequential glycosylation of Drosophila EGF20 in vitro by EOGT, β4GalT-1, and ST3Gal-IV. Thus, the findings from our study throw light on the specific glycosyltransferases that mediate O-GlcNAc glycan elongation in human HEK293 cells.
AB - O-GlcNAc is a unique post-translational modification found in cytoplasmic, nuclear, and mitochondrial proteins. In a limited number of extracellular proteins, O-GlcNAc modifications occur through the action of EOGT, which specifically modifies subsets of epidermal growth factor-like (EGF) domain-containing proteins such as Notch receptors. The abnormalities due to EOGT mutations in mice and humans and the increased EOGT expression in several cancers signify the importance of EOGT pathophysiology and extracellular O-GlcNAc. Unlike intracellular O-GlcNAc monosaccharides, extracellular O-GlcNAc extends to form elongated glycan structures. However, the enzymes involved in the O-GlcNAc glycan extension have not yet been reported. In our study, we comprehensively screened potential galactosyltransferase and sialyltransferase genes related to the canonical O-GlcNAc glycan pathway and revealed the essential roles of B4GALT1 and ST3GAL4 in O-GlcNAc glycan elongation in human HEK293 cells. These findings were confirmed by sequential glycosylation of Drosophila EGF20 in vitro by EOGT, β4GalT-1, and ST3Gal-IV. Thus, the findings from our study throw light on the specific glycosyltransferases that mediate O-GlcNAc glycan elongation in human HEK293 cells.
KW - B4GALT1
KW - Notch
KW - O-GlcNAc
KW - ST3GAL4
U2 - 10.1016/j.bbrc.2024.149610
DO - 10.1016/j.bbrc.2024.149610
M3 - Journal article
C2 - 38359610
AN - SCOPUS:85185841498
VL - 703
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
M1 - 149610
ER -
ID: 384489857