The Role of Glycosylation in Receptor Signaling

Arey, Brian J.

doi:10.5772/50262

Cited by 5 publications

(4 citation statements)

References 59 publications

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“…Proper functioning of proteins depends greatly on the post-translational modifications (PTMs) of proteins, glycosylation and phosphorylation being major two. In this regard, the glycosylation process plays a major role in protein folding, stability and signal transduction (Arey, 2012), whereas phosphorylation plays a critical role in the activation or deactivation of proteins by altering structural conformation (Cohen, 2002) and plays a significant role in the signaling pathways (Cutillas, 2017), metabolism and in combating various stress conditions (Zhang et al, 2020). In response to abiotic stresses in crop plants, PTM of proteins have been reported in response to abiotic stresses in crop plants and is suggested to be involved in various biological processes under natural conditions (Wu et al, 2016).…”

Section: Discussionmentioning

confidence: 99%

Comprehensive in silico Characterization of Universal Stress Proteins in Rice (Oryza sativa L.) With Insight Into Their Stress-Specific Transcriptional Modulation

et al. 2021

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In a world where climate change is real and its consequences are unprecedented, understanding of the plant adaptive capacity and native stress-responsive machinery is crucial. In recent years, universal stress proteins (USPs) have received much attention in the field of plant science due to their stress-specific transcriptional regulation. This study focuses on the extensive characterization of the USP gene family members in the monocot crop rice (Oryza sativa L. var. japonica). Here, we report a total of 44 USP genes in the rice genome. In silico characterization of these genes showed that domain architecture played a major role in the functional diversification of the USP gene family which holds for all plant USPs. On top of that, a higher conservation of OsUSP members has been exhibited with a monocot genome (Zea mays L.) as compared to a dicot genome (Arabidopsis thaliana L.). Expression profiling of the identified genes led to the discovery of multiple OsUSP genes that showed pronounced transcript alteration under various abiotic stress conditions, indicating their potential role as multi-functional stress-specific modules. Furthermore, expression validation of OsUSP genes using qRT-PCR provided a strong evidence for the utility OsUSP genes in building multi-stress tolerant plants. Altogether, this study provides leads to suitable USP candidates that could be targeted for plant breeding and genetic engineering experiments to develop stress resilient crop species.

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Section: Discussionmentioning

confidence: 99%

Comprehensive in silico Characterization of Universal Stress Proteins in Rice (Oryza sativa L.) With Insight Into Their Stress-Specific Transcriptional Modulation

et al. 2021

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“…In any cancer treatment, the development of drug resistance seems to be almost imminent, and this limiting factor prevents the achievement of cures in patients with cancers [ 25 ]. The aberrant glycosylation is one of the leading factors in developing drug resistance phenotypes in cancer cells [ 26 ]. Some oncoproteins and oncogenes promote aggressive phenotypes such as proliferation and drug resistance via N-linked glycosylation [ 27 , 28 ].…”

Section: How Does Tunicamycin Work?mentioning

confidence: 99%

Benefits and Pitfalls of a Glycosylation Inhibitor Tunicamycin in the Therapeutic Implication of Cancers

Banerjee,

Ansari,

Upadhyay

et al. 2024

Cells

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The aberrant glycosylation is a hallmark of cancer progression and chemoresistance. It is also an immune therapeutic target for various cancers. Tunicamycin (TM) is one of the potent nucleoside antibiotics and an inhibitor of aberrant glycosylation in various cancer cells, including breast cancer, gastric cancer, and pancreatic cancer, parallel with the inhibition of cancer cell growth and progression of tumors. Like chemotherapies such as doxorubicin (DOX), 5′fluorouracil, etoposide, and cisplatin, TM induces the unfolded protein response (UPR) by blocking aberrant glycosylation. Consequently, stress is induced in the endoplasmic reticulum (ER) that promotes apoptosis. TM can thus be considered a potent antitumor drug in various cancers and may promote chemosensitivity. However, its lack of cell-type-specific cytotoxicity impedes its anticancer efficacy. In this review, we focus on recent advances in our understanding of the benefits and pitfalls of TM therapies in various cancers, including breast, colon, and pancreatic cancers, and discuss the mechanisms identified by which TM functions. Finally, we discuss the potential use of nano-based drug delivery systems to overcome non-specific toxicity and enhance the therapeutic efficacy of TM as a targeted therapy.

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“…[4,5] This is due to the fact that most protein chemistry methods work mainly,ifn ot exclusively,i nw ater-based media, whereas membrane proteins require ab alanced hydrophilic and lipophilic environment. In addition, although membranep rotein glycosylationa nd its role in receptor signaling are emerging topics, [6] the identification of protein glycosylation sites and the deconvolution of the monosaccharide compositiono ns pecific membrane-bound proteins are challenging. [7] For membrane proteomic studies, the irreversible attachmento fachemical reportert oaligand's membrane-proteint arget greatlyf acilitates protein characterization, isolation andb ioanalysis.…”

mentioning

confidence: 99%

“…However,amolecular characteristic that is shared among almost all cell-surface membrane proteins is glycosylation, which is highly abundant on virtually every cell type. [6,10] Because azidosugars can be easily incorporated into cell-surface glycans by metabolic glycane ngineering, [11] we hypothesized that the Huisgen 1,3-dipolar cycloadditionb etween azides and acetylenes offers an attractive alternative to traditional crosslinkingm ethods (Scheme 1). The required biorthogonal alkyl functional groups are fully compatible with biomolecules under physiological conditions, [12] and the reactioni s driven by the relative proximity of the reactants in the ligandbound state relative to bulk concentration.…”

mentioning

confidence: 99%

Glycan‐Mediated, Ligand‐Controlled Click Chemistry for Drug‐Target Identification

et al. 2015

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Membrane-bound proteins are important pharmaceutical drug targets, yet few strategies exist for the identification of small-molecule-targeted membrane proteins in live-cell systems. By exploiting metabolic glycan engineering of cell membrane proteins, we have developed an in situ glycan-mediated ligand-controlled click ("GLiCo-Click") chemistry methodology that enables the attachment of small-molecule chemical probes to their receptor protein through glycans on live cells. In addition to enabling receptor enrichment from cell lysates, this strategy can be used to demonstrate target receptor engagement and enables the molecular characterization of receptors.

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The Role of Glycosylation in Receptor Signaling

Cited by 5 publications

References 59 publications

Comprehensive in silico Characterization of Universal Stress Proteins in Rice (Oryza sativa L.) With Insight Into Their Stress-Specific Transcriptional Modulation

Comprehensive in silico Characterization of Universal Stress Proteins in Rice (Oryza sativa L.) With Insight Into Their Stress-Specific Transcriptional Modulation

Benefits and Pitfalls of a Glycosylation Inhibitor Tunicamycin in the Therapeutic Implication of Cancers

Glycan‐Mediated, Ligand‐Controlled Click Chemistry for Drug‐Target Identification

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