Mori, Kento

写真a

Affiliation

Faculty of Science and Technology, Department of Applied Chemistry (Yagami)

Position

Assistant Professor (Non-tenured)/Research Associate (Non-tenured)/Instructor (Non-tenured)

Academic Degrees 【 Display / hide

  • Doctor (Science), Keio University, Coursework, 2022.03

 

Papers 【 Display / hide

  • Involvement of dpy19l3 in myogenic differentiation of c2c12 myoblasts

    Mori K., Sun H., Miura K., Simizu S.

    Molecules (Molecules)  26 ( 18 )  2021.09

     View Summary

    DPY19L3 has been identified as a C-mannosyltransferase for thrombospondin type-1 repeat domain-containing proteins. In this study, we focused on the role of DPY19L3 in the myogenic differentiation of C2C12 mouse myoblast cells. We carried out DPY19L3 gene depletion using the CRISPR/Cas9 system. The result showed that these DPY19L3-knockout cells could not be induced for differentiation. Moreover, the phosphorylation levels of MEK/ERK and p70S6K were suppressed in the DPY19L3-knockout cells compared with that of parent cells, suggesting that the protein(s) that is(are) DPY19L3-mediated C-mannosylated and regulate(s) MEK/ERK or p70S6K signaling is(are) required for the differentiation.

  • Involvement of LH3 and GLT25D1 for glucosyl-galactosyl-hydroxylation on non-collagen-like domain of FGL1

    Mori K., Suzuki T., Miura K., Dohmae N., Simizu S.

    Biochemical and Biophysical Research Communications (Biochemical and Biophysical Research Communications)  560   93 - 98 2021.06

    ISSN  0006291X

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    Glucosyl-galactosyl-hydroxylation (GGH) is one type of post-translational modification, which is mainly observed in collagen-like domain-containing proteins. Using LC-MS/MS analysis, we found a GGH-like modification at Lys65 of fibrinogen-like protein 1 (FGL1), although it does not contain a collagen-like domain. To identify the glycosyltransferases responsible for this modification, we established LH3/GLT25D1-knockout FGL1-overexpressing HT1080 cell lines. The result showed that knockout of LH3 or GLT25D1 significantly inhibited the glycosylation. Furthermore, deficiency of GGH by point mutation of the FGL1 protein or knockout of the GGH-related glycosyltransferase reduced FGL1 protein levels. Taken together, these data indicate that Lys65 of FGL1 is glucosyl-galactosyl-hydroxylated by LH3 and GLT25D1. Our results provide novel insights to regulate various FGL1 functions.

  • The fibrinogen C-terminal domain is seldom C-mannosylated but its C-mannosylation is important for the secretion of microfibril-associated glycoprotein 4

    Osada Y., Suzuki T., Mizuta H., Mori K., Miura K., Dohmae N., Simizu S.

    Biochimica et Biophysica Acta - General Subjects (Biochimica et Biophysica Acta - General Subjects)  1864 ( 9 )  2020.09

    ISSN  03044165

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    Background: C-mannosylation is the one of glycosylations. Microfibril-associated glycoprotein 4 (MFAP4), an important protein for tissue homeostasis and cell adhesion, contains a consensus sequence of C-mannosylation in its fibrinogen C-terminal domain. In this study, we sought to demonstrate that fibrinogen C-terminal domain is a new substrate domain for C-mannosylation. Methods: We established an MFAP4-overexpresssing HT1080 cell line and purified recombinant MFAP4 protein from the conditioned medium for LC-MS/MS analysis. Subcellular localization of MFAP4 was observed under confocal fluorescence microscope. Results: We found that MFAP4 is C-mannosylated at Trp235 in the fibrinogen C-terminal domain by LC-MS/MS. To determine the functions of the C-mannosylation of MFAP4, we established a C-mannosylation-defective mutant MFAP4-overexpresssing HT1080 cell line and measured its secretion of MFAP4. The secretion of MFAP4 decreased significantly in the C-mannosylation-defective mutant MFAP4-overexpresssing cell line versus wild-type cells. Moreover, co-transfection experiments indicated that C-mannosylated MFAP4 accelerated its secretion. Conclusions: Our results demonstrate that the fibrinogen C-terminal domain is a novel C-mannosylation domain and that the C-mannosylation of MFAP4 is important for its secretion. General significance: These results suggest that C-mannosylation has a role for dominant effect for MFAP4 secretion.

 

Courses Taught 【 Display / hide

  • LABORATORY IN SCIENCE

    2022

  • LABORATORIES IN APPLIED CHEMISTRY D

    2022

  • LABORATORY IN SCIENCE

    2021

  • LABORATORIES IN APPLIED CHEMISTRY D

    2021