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Related Concept Videos

Protein Modifications in the RER01:26

Protein Modifications in the RER

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
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Peroxisomes01:24

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Peroxisomes are specialized organelles present in fungi, plant, and animal cells. It can vary in number, size, morphology, and activity depending on the type of tissue and the nutritional state of the cell. For example, cells with active lipid metabolism, such as adipocytes, neurons, and hepatocytes, have more peroxisomes than other cells in the body. Besides their primary role in breaking down complex organic molecules, peroxisomes can also synthesize specific macromolecules and participate in...
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Related Experiment Video

Updated: Oct 10, 2025

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
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Sirtuin Oxidative Post-translational Modifications.

Kelsey S Kalous1, Sarah L Wynia-Smith1, Brian C Smith1

  • 1Department of Biochemistry, Medical College of Wisconsin, Milwaukee, WI, United States.

Frontiers in Physiology
|December 13, 2021
PubMed
Summary
This summary is machine-generated.

Cellular oxidants, such as reactive oxygen and nitrogen species (ROS/RNS), inhibit sirtuin deacylase activity, contributing to aging and disease. Preventing this oxidative modification may boost sirtuin activity during aging.

Keywords:
glutathionylationnitrationnitrosationnitrosylationoxidationsirtuin (SIRT)sulfenylationsulfhydration

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Area of Science:

  • Biochemistry
  • Gerontology
  • Molecular Biology

Background:

  • Sirtuin deacylase activity is crucial for lifespan and healthspan, with decreased activity linked to aging-related diseases.
  • Mechanisms behind reduced sirtuin activity during aging are not fully understood.
  • Oxidative post-translational modifications by reactive oxygen species (ROS) and reactive nitrogen species (RNS) inhibit sirtuin activity.

Purpose of the Study:

  • To explore the role of cellular oxidants in inhibiting human sirtuin isoforms.
  • To clarify the relevance of ROS/RNS in regulating sirtuin activity in health and disease.

Main Methods:

  • Review of existing literature on sirtuin deacylase activity.
  • Analysis of oxidative post-translational modifications (nitrosation, glutathionylation, sulfenylation, sulfhydration, nitration) of sirtuins.
  • Examination of ROS/RNS prevalence in aging and inflammation.

Main Results:

  • ROS/RNS, including nitric oxide, S-nitrosoglutathione, hydrogen peroxide, oxidized glutathione, and peroxynitrite, inhibit sirtuin deacylase activity.
  • Increased ROS/RNS production with age and during inflammation contributes to sirtuin inhibition.
  • Oxidative modification of sirtuins by ROS/RNS may link aging, inflammation, and disease.

Conclusions:

  • Cellular oxidants play a significant role in decreasing sirtuin activity during aging.
  • Preventing inhibitory oxidative modifications of sirtuins offers a potential strategy to enhance sirtuin activity and combat aging-related diseases.