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Related Concept Videos

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
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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.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
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Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

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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 Unfolded Protein Response01:37

The Unfolded Protein Response

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The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
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Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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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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Related Experiment Video

Updated: May 6, 2026

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
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Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates

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SIRT6, a protein with many faces.

Asaf A Gertler1, Haim Y Cohen

  • 1The Mina & Everard Goodman Faculty of Life Sciences, Bar-Ilan University, 52900, Ramat-Gan, Israel.

Biogerontology
|November 12, 2013
PubMed
Summary

Sirtuins are enzymes regulating cellular processes. This review highlights recent discoveries about SIRT6, a key enzyme in healthy aging, detailing its functions and pathways.

Area of Science:

  • Biochemistry and Molecular Biology
  • Cellular Biology
  • Aging Research

Background:

  • Sirtuins are a class of NAD(+)-dependent deacylases with diverse cellular functions.
  • Mammalian sirtuins (SIRT1-SIRT7) exhibit distinct subcellular localizations and catalytic activities.
  • SIRT6 has emerged as a critical regulator of healthy aging.

Purpose of the Study:

  • To review recent advancements in understanding the SIRT6 enzyme.
  • To consolidate knowledge on SIRT6's cellular localization, catalytic functions, substrates, and associated pathways.

Main Methods:

  • Literature review of recent scientific publications on SIRT6.
  • Analysis of experimental data and findings related to SIRT6 activity and regulation.

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Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve
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An Integrated Approach for Microprotein Identification and Sequence Analysis
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An Integrated Approach for Microprotein Identification and Sequence Analysis

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Related Experiment Videos

Last Updated: May 6, 2026

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
14:32

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Published on: February 27, 2016

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Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve
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Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve

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An Integrated Approach for Microprotein Identification and Sequence Analysis
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An Integrated Approach for Microprotein Identification and Sequence Analysis

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Main Results:

  • Significant progress has been made in elucidating SIRT6's role in cellular homeostasis.
  • Detailed understanding of SIRT6's substrates and involvement in key metabolic and DNA repair pathways.

Conclusions:

  • SIRT6 is a pivotal enzyme in the biology of aging.
  • Continued research on SIRT6 promises new insights into age-related diseases and interventions.