scholarly journals The Role of Stress-Induced O-GlcNAc Protein Modification in the Regulation of Membrane Transport

2017 ◽  
Vol 2017 ◽  
pp. 1-15 ◽  
Author(s):  
Viktória Fisi ◽  
Attila Miseta ◽  
Tamás Nagy
Keyword(s):  
Membrane Trafficking ◽  
Posttranslational Modification ◽  
Protein Modification ◽  
Protein Transport ◽  
Feedback Mechanism ◽  
Current Data ◽  
Nutrient Sensing ◽  
Exact Nature ◽  
Reversible Process

O-linked N-acetylglucosamine (O-GlcNAc) is a posttranslational modification that is increasingly recognized as a signal transduction mechanism. Unlike other glycans, O-GlcNAc is a highly dynamic and reversible process that involves the addition and removal of a single N-acetylglucosamine molecule to Ser/Thr residues of proteins. UDP-GlcNAc—the direct substrate for O-GlcNAc modification—is controlled by the rate of cellular metabolism, and thus O-GlcNAc is dependent on substrate availability. Serving as a feedback mechanism, O-GlcNAc influences the regulation of insulin signaling and glucose transport. Besides nutrient sensing, O-GlcNAc was also implicated in the regulation of various physiological and pathophysiological processes. Due to improvements of mass spectrometry techniques, more than one thousand proteins were detected to carry the O-GlcNAc moiety; many of them are known to participate in the regulation of metabolites, ions, or protein transport across biological membranes. Recent studies also indicated that O-GlcNAc is involved in stress adaptation; overwhelming evidences suggest that O-GlcNAc levels increase upon stress. O-GlcNAc elevation is generally considered to be beneficial during stress, although the exact nature of its protective effect is not understood. In this review, we summarize the current data regarding the oxidative stress-related changes of O-GlcNAc levels and discuss the implications related to membrane trafficking.

scholarly journals RINT-1 Regulates the Localization and Entry of ZW10 to the Syntaxin 18 Complex

2006 ◽  
Vol 17 (6) ◽  
pp. 2780-2788 ◽  
Author(s):  
Kohei Arasaki ◽  
May Taniguchi ◽  
Katsuko Tani ◽  
Mitsuo Tagaya
Keyword(s):  
Endoplasmic Reticulum ◽  
Membrane Trafficking ◽  
Protein Transport ◽  
Snare Complex ◽  
Checkpoint Control ◽  
Interacting Protein ◽  
Golgi Transport ◽  
Radiation Induced ◽  
And Function

RINT-1 was first identified as a Rad50-interacting protein that participates in radiation-induced G2/M checkpoint control. We have recently reported that RINT-1, together with the dynamitin-interacting protein ZW10 and others, is associated with syntaxin 18, an endoplasmic reticulum (ER)-localized SNARE involved in membrane trafficking between the ER and Golgi. To address the role of RINT-1 in membrane trafficking, we examined the effects of overexpression and knockdown of RINT-1 on Golgi morphology and protein transport from the ER. Overexpression of the N-terminal region of RINT-1, which is responsible for the interaction with ZW10, caused redistribution of ZW10. Concomitantly, ER-to-Golgi transport was blocked and the Golgi was dispersed. Knockdown of RINT-1 also disrupted membrane trafficking between the ER and Golgi. Notably, silencing of RINT-1 resulted in a reduction in the amount of ZW10 associated with syntaxin 18, concomitant with ZW10 redistribution. In contrast, no redistribution or release of RINT-1 from the syntaxin 18 complex was observed when ZW10 expression was reduced. These results taken together suggest that RINT-1 coordinates the localization and function of ZW10 by serving as a link between ZW10 and the SNARE complex comprising syntaxin 18.

scholarly journals Activity and Trafficking of Copper-Transporting ATPases in Tumor Development and Defense against Platinum-Based Drugs

Cells ◽  
2019 ◽  
Vol 8 (9) ◽  
pp. 1080 ◽  
Author(s):  
Raffaella Petruzzelli ◽  
Roman S. Polishchuk
Keyword(s):  
Tumor Cells ◽  
Membrane Trafficking ◽  
Tumor Development ◽  
Current Data ◽  
Malignant Cells ◽  
Potential Toxicity ◽  
Cellular Processes ◽  
Wide Range ◽  
Cu Homeostasis

Membrane trafficking pathways emanating from the Golgi regulate a wide range of cellular processes. One of these is the maintenance of copper (Cu) homeostasis operated by the Golgi-localized Cu-transporting ATPases ATP7A and ATP7B. At the Golgi, these proteins supply Cu to newly synthesized enzymes which use this metal as a cofactor to catalyze a number of vitally important biochemical reactions. However, in response to elevated Cu, the Golgi exports ATP7A/B to post-Golgi sites where they promote sequestration and efflux of excess Cu to limit its potential toxicity. Growing tumors actively consume Cu and employ ATP7A/B to regulate the availability of this metal for oncogenic enzymes such as LOX and LOX-like proteins, which confer higher invasiveness to malignant cells. Furthermore, ATP7A/B activity and trafficking allow tumor cells to detoxify platinum (Pt)-based drugs (like cisplatin), which are used for the chemotherapy of different solid tumors. Despite these noted activities of ATP7A/B that favor oncogenic processes, the mechanisms that regulate the expression and trafficking of Cu ATPases in malignant cells are far from being completely understood. This review summarizes current data on the role of ATP7A/B in the regulation of Cu and Pt metabolism in malignant cells and outlines questions and challenges that should be addressed to understand how ATP7A and ATP7B trafficking mechanisms might be targeted to counteract tumor development.

scholarly journals Role of Glycoproteins during Fruit Ripening and Seed Development

Cells ◽  
2021 ◽  
Vol 10 (8) ◽  
pp. 2095
Author(s):  
Angela Mendez-Yañez ◽  
Patricio Ramos ◽  
Luis Morales-Quintana
Keyword(s):  
Posttranslational Modifications ◽  
Fruit Ripening ◽  
Posttranslational Modification ◽  
Protein Modification ◽  
Secretory Pathway ◽  
Plant Cells ◽  
Protein Glycosylation ◽  
Cellular Processes ◽  
Fruit Development And Ripening

Approximately thirty percent of the proteins synthesized in animal or plant cells travel through the secretory pathway. Seventy to eighty percent of those proteins are glycosylated. Thus, glycosylation is an important protein modification that is related to many cellular processes, such as differentiation, recognition, development, signal transduction, and immune response. Additionally, glycosylation affects protein folding, solubility, stability, biogenesis, and activity. Specifically, in plants, glycosylation has recently been related to the fruit ripening process. This review aims to provide valuable information and discuss the available literature focused on three principal topics: (I) glycosylations as a key posttranslational modification in development in plants, (II) experimental and bioinformatics tools to analyze glycosylations, and (III) a literature review related to glycosylations in fruit ripening. Based on these three topics, we propose that it is necessary to increase the number of studies related to posttranslational modifications, specifically protein glycosylation because the specific role of glycosylation in the posttranslational process and how this process affects normal fruit development and ripening remain unclear to date.

Modern methods of treating rosacea

2019 ◽  
Vol 1 (7) ◽  
pp. 65-71
Author(s):  
O. A. Egorova ◽  
K. A. Novikov
Keyword(s):  
Clinical Manifestations ◽  
Treatment Method ◽  
Current Data ◽  
Trigger Factors ◽  
Laser Technology ◽  
Individual Approach ◽  
Modern Methods ◽  
Methods Of Treatment ◽  
Choice Of Therapy

Presented current data on the etiology of rosacea, the main aspects of pathogenesis, clinical forms of the disease. Reflects trigger factors leading to rosacea, as well as complicating its course. Modern methods of treatment are described, including the use of new safe preparations of ivermectin and brimonidine, providing a good, lasting effect of clinical manifestations of rosacea. The role of laser technology, actively occupying a leading place in the choice of physiotherapeutic treatment method, is noted. The need for an individual approach in the choice of therapy for each patient with rosacea is emphasized.

scholarly journals Small GTPases of the Rab and Arf Families: Key Regulators of Intracellular Trafficking in Neurodegeneration

2021 ◽  
Vol 22 (9) ◽  
pp. 4425
Author(s):  
Alazne Arrazola Arrazola Sastre ◽  
Miriam Luque Luque Montoro ◽  
Hadriano M. Lacerda ◽  
Francisco Llavero ◽  
José L. Zugaza
Keyword(s):  
Membrane Trafficking ◽  
Neurodegenerative Disorders ◽  
Synaptic Vesicles ◽  
Intracellular Trafficking ◽  
Small Gtpases ◽  
Constant Flow ◽  
Parkinson’S Diseases ◽  
The Central Nervous System ◽  
Arf Gtpases

Small guanosine triphosphatases (GTPases) of the Rab and Arf families are key regulators of vesicle formation and membrane trafficking. Membrane transport plays an important role in the central nervous system. In this regard, neurons require a constant flow of membranes for the correct distribution of receptors, for the precise composition of proteins and organelles in dendrites and axons, for the continuous exocytosis/endocytosis of synaptic vesicles and for the elimination of dysfunctional proteins. Thus, it is not surprising that Rab and Arf GTPases have been associated with neurodegenerative diseases such as Alzheimer’s and Parkinson’s. Both pathologies share characteristics such as the presence of protein aggregates and/or the fragmentation of the Golgi apparatus, hallmarks that have been related to both Rab and Arf GTPases functions. Despite their relationship with neurodegenerative disorders, very few studies have focused on the role of these GTPases in the pathogenesis of neurodegeneration. In this review, we summarize their importance in the onset and progression of Alzheimer’s and Parkinson’s diseases, as well as their emergence as potential therapeutical targets for neurodegeneration.

scholarly journals Histone Deacetylase Enzymes as Potential Drug Targets in Cancer and Parasitic Diseases

2006 ◽  
Vol 2006 ◽  
pp. 1-10 ◽  
Author(s):  
Mehdi Ouaissi ◽  
Ali Ouaissi
Keyword(s):  
Transcriptional Activation ◽  
Histone Deacetylases ◽  
Drug Targets ◽  
Large Family ◽  
Current Data ◽  
Functional Study ◽  
Parasitic Diseases ◽  
Antitumor Effects ◽  
Protozoan Infections

The elucidation of the mechanisms of transcriptional activation and repression in eukaryotic cells has shed light on the important role of acetylation-deacetylation of histones mediated by histone acetyltransferases (HATs) and histone deacetylases (HDACs), respectively. Another group belonging to the large family of sirtuins (silent information regulators (SIRs)) has an (nicotinamide adenine dinucleotide)NAD+-dependent HDAC activity. Several inhibitors of HDACs (HDIs) have been shown to exert antitumor effects. Interestingly, some of the HDIs exerted a broad spectrum of antiprotozoal activity. The purpose of this review is to analyze some of the current data related to the deacetylase enzymes as a possible target for drug development in cancer and parasitic diseases with special reference to protozoan infections. Given the structural differences among members of this family of enzymes, development of specific inhibitors will not only allow selective therapeutic intervention, but may also provide a powerful tool for functional study of these enzymes.

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