Human immunodeficiency virus type 1: Role of proteins in the context of viral life cycle

Jha, Vikas; Rustagi, Kush; Gharat, Kunal; Sonawane, Neetu; Rathod, Meet; Patel, Reetikesh; Devkar, Sakshi; Dhamapurkar, Vrushali; Kaur, Navdeep

doi:10.5455/jabet.2022.d117

J Adv Biotechnol Exp Ther

2022

DOI: 10.5455/jabet.2022.d117

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Human immunodeficiency virus type 1: Role of proteins in the context of viral life cycle

Vikas Jha¹,

Kush Rustagi²,

Kunal Gharat³

et al.

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2023

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“…For example, it is essential for the oncogenic activity of the Src protein, which is a major molecule in cancer (7). In addition to cancer, this lipid modification is related to immune disorders, such as human immunodeficiency virus (HIV) infection and fungus activation (8)(9)(10). Although PTM are important in mediating the immune system, detection methods for myristoylation have not been established compared to those for other PTMs for a long time.…”

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confidence: 99%

TNF-α-induced Inhibition of Protein MyristoylationViaBinding Between NMT1 and Sorbs2 in Osteoblasts

KUTSUNA,

SUGIYAMA,

KOMIYAMA

et al. 2023

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Background/Aim: Bone resolution due to tumor invasion often occurs on the surface of the jaw and is important for clinical prognosis. Although cytokines, such as TNF-α are known to impair osteoblasts, the underlying mechanism remains unclear. Protein myristoylation, a posttranslational modification, plays an important role in the development of immune responses and cancerization of cells. A clear understanding of the mechanisms underlying this involvement will provide insights into molecular-targeted therapies. N-myristoyltransferase1 (NMT1), a specific enzyme involved in myristoylation, is expressed in cancer cells and in other normal cells, suggesting that changes in myristoylation may result from the regulation of NMT1 in cancer cells. Materials and Methods: Using newly emerging state-of-the-art techniques such as the Click-it assay, RNA interference, mass spectrometry, immunoprecipitation, immunocytochemistry, and western blotting, the expression of myristoylated proteins and the role of TNF-α stimulation on NMT1 and Sorbs2 binding were evaluated in a murine osteoblastic cell line (MC3T3-E1). Results: The expression of myristoylated proteins was detected; however, TNF-α stimulation resulted in their inhibition in MC3T3-E1 cells. The expression of NMT1 also increased. Immunoprecipitation and mass spectrometry identified Sorbs2 as a novel binding protein of NMT1, which upon TNF-α stimulation, inhibited myristoylation. Conclusion: The binding between NMT1 and Sorbs2 can regulate myristoylation, and NMT1 can be considered as a potential target molecule for tumor invasion.

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mentioning

confidence: 99%

TNF-α-induced Inhibition of Protein MyristoylationViaBinding Between NMT1 and Sorbs2 in Osteoblasts

KUTSUNA,

SUGIYAMA,

KOMIYAMA

et al. 2023

In Vivo

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Human immunodeficiency virus type 1: Role of proteins in the context of viral life cycle

Cited by 1 publication

References 0 publications

TNF-α-induced Inhibition of Protein MyristoylationViaBinding Between NMT1 and Sorbs2 in Osteoblasts

TNF-α-induced Inhibition of Protein MyristoylationViaBinding Between NMT1 and Sorbs2 in Osteoblasts

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