Secretory expression of mammalian NOTCH tandem epidermal growth factor-like repeats based on increased O-glycosylation

Zhang, Ailing; Tsukamoto, Yohei; Takeuchi, Hideyuki; Nishiwaki, Kimitoshi; Tashima, Yohtalou; Okajima, Tetsuya

doi:10.1016/j.ab.2022.114881

Cited by 3 publications

(1 citation statement)

References 27 publications

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“…GlcNAc-β-Asn OST complex (STT3A/ STT3B) N-X-T/S, X≠P N-G; N-X-C/V, X≠P None Protein stability, 1118 protein folding and quality control, 1119 self/nonself recognition, 1120 cell adhesion 1121 , immunotherapy, 1122 receptor activation and endocytosis, 1123 glycoediting and drug delivery. 1124 O-glycosylation GalNAc-α-Ser/Thr GALNT1-20 Weak isoform specific motifs 1093 None O-glycan shielding is essential for secretion of an active protein, 1125 participates in immunological recognition of the immune system, 1082 protects membrane proteins from ectodomain shedding, 1090 increases the half-life of peptide hormones in circulation, 1126 modulates the interaction between viral proteins and host surface receptors. 1127 O-glycosylated mucins expressed at mucosal surfaces such as the respiratory and GI tract can form an effective barrier against pathogens.…”

Section: N-glycosylationmentioning

confidence: 99%

Protein posttranslational modifications in health and diseases: Functions, regulatory mechanisms, and therapeutic implications

Zhong

Xiao

Xie

et al. 2023

MedComm

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Protein posttranslational modifications (PTMs) refer to the breaking or generation of covalent bonds on the backbones or amino acid side chains of proteins and expand the diversity of proteins, which provides the basis for the emergence of organismal complexity. To date, more than 650 types of protein modifications, such as the most well‐known phosphorylation, ubiquitination, glycosylation, methylation, SUMOylation, short‐chain and long‐chain acylation modifications, redox modifications, and irreversible modifications, have been described, and the inventory is still increasing. By changing the protein conformation, localization, activity, stability, charges, and interactions with other biomolecules, PTMs ultimately alter the phenotypes and biological processes of cells. The homeostasis of protein modifications is important to human health. Abnormal PTMs may cause changes in protein properties and loss of protein functions, which are closely related to the occurrence and development of various diseases. In this review, we systematically introduce the characteristics, regulatory mechanisms, and functions of various PTMs in health and diseases. In addition, the therapeutic prospects in various diseases by targeting PTMs and associated regulatory enzymes are also summarized. This work will deepen the understanding of protein modifications in health and diseases and promote the discovery of diagnostic and prognostic markers and drug targets for diseases.

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Section: N-glycosylationmentioning

confidence: 99%

Protein posttranslational modifications in health and diseases: Functions, regulatory mechanisms, and therapeutic implications

Zhong

Xiao

Xie

et al. 2023

MedComm

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Characterization of galactosyltransferase and sialyltransferase genes mediating the elongation of the extracellular O-GlcNAc glycans

Tsukamoto,

Saiki

et al. 2024

Biochemical and Biophysical Research Communications

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The glycosyltransferase POGLUT1 regulates muscle stem cell development and maintenance in mice

Cho,

Servián-Morilla,

Garrido

et al. 2024

Preprint

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Mutations in proteinO-glucosyltransferase 1 (POGLUT1) cause a recessive form of limb-girdle muscular dystrophy (LGMD-R21) associated with reduced satellite cell number and NOTCH1 signaling in adult patient muscles and impaired myogenic capacity of patient-derived muscle progenitors. However, thein vivoroles of POGLUT1 in the development, function, and maintenance of satellite cells are not well understood. Here, we show that conditional deletion of mousePoglut1in myogenic progenitors leads to early lethality, postnatal muscle growth defects, reducedPax7expression, abnormality in muscle extracellular matrix, and impaired muscle repair.Poglut1-deficient muscle progenitors exhibit reduced proliferation, enhanced differentiation, and accelerated fusion into myofibers. Inducible loss ofPoglut1in adult satellite cells leads to their precocious differentiation and impairs muscle repair upon serial injury. Cell-based signaling assays and mass spectrometric analysis indicate that POGLUT1 is required for the activation of NOTCH1, NOTCH2, and NOTCH3 in myoblasts and that NOTCH3 is a target of POGLUT1 like NOTCH1 and NOTCH2. These observations provide insight into the roles of POGLUT1 in muscle development and repair and the pathophysiology of LGMD-R21.

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Secretory expression of mammalian NOTCH tandem epidermal growth factor-like repeats based on increased O-glycosylation

Cited by 3 publications

References 27 publications

Protein posttranslational modifications in health and diseases: Functions, regulatory mechanisms, and therapeutic implications

Protein posttranslational modifications in health and diseases: Functions, regulatory mechanisms, and therapeutic implications

Characterization of galactosyltransferase and sialyltransferase genes mediating the elongation of the extracellular O-GlcNAc glycans

The glycosyltransferase POGLUT1 regulates muscle stem cell development and maintenance in mice

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