Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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.
These groups modify specific amino acids in a protein.
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

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 rapamycin-insensitive companion...
Regulation of Metabolism01:19

Regulation of Metabolism

Cellular needs and conditions vary from cell to cell and change within individual cells over time. For example, the required enzymes and energetic demands of stomach cells are different from those of fat storage cells, skin cells, blood cells, and nerve cells. Furthermore, a digestive cell works much harder to process and break down nutrients during the time that closely follows a meal compared with many hours after a meal. As these cellular demands and conditions vary, so do the amounts and...
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

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...
mTOR Signaling and Cancer Progression03:03

mTOR Signaling and Cancer Progression

The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
The mTOR pathway or the...
Regulated Protein Degradation02:58

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

dCas9-metabolic enzyme fusions modulate global and locus-specific gene expression.

bioRxiv : the preprint server for biology·2026
Same author

Reciprocal E-cadherin signaling aligns apical surfaces between neighboring epithelial tissues to complete the C. elegans digestive tract.

Current biology : CB·2026
Same author

Genetic loss of CHD1 regulates distinct histone post-translational modifications in the development of castration-resistant prostate cancer.

Neoplasia (New York, N.Y.)·2026
Same author

Histone-modifying enzymes as drivers and therapeutic targets in androgen-resistant prostate cancer.

Frontiers in endocrinology·2026
Same author

Depletion of individual dietary amino acids induce distinct metabolic and chromatin states.

The Journal of biological chemistry·2025
Same author

Inactivation of microtubule organizing center function of the centrosome is required for neuronal development and centriole elimination.

bioRxiv : the preprint server for biology·2025

Related Experiment Video

Updated: May 17, 2026

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

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

Published on: February 27, 2016

Sirtuin catalysis and regulation.

Jessica L Feldman1, Kristin E Dittenhafer-Reed, John M Denu

  • 1Department of Biomolecular Chemistry and the Wisconsin Institute for Discovery, University of Wisconsin, Madison, Wisconsin 53715, USA. jmdenu@wisc.edu

The Journal of Biological Chemistry
|October 23, 2012
PubMed
Summary
This summary is machine-generated.

Sirtuins, NAD(+)-dependent enzymes, regulate key cellular processes and are linked to health span and disease. This review covers their chemistry, targets, regulation, and the development of small-molecule drugs.

Related Experiment Videos

Last Updated: May 17, 2026

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

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

Published on: February 27, 2016

Area of Science:

  • Biochemistry and Molecular Biology
  • Cellular Biology
  • Pharmacology

Background:

  • Sirtuins are NAD(+)-dependent enzymes regulating transcription, metabolism, and stress response.
  • These enzymes are implicated in aging, caloric restriction pathways, and various human diseases.
  • Therapeutic targeting of sirtuins is of significant interest due to their health implications.

Purpose of the Study:

  • To review the current understanding of sirtuin enzyme catalysis and biological functions.
  • To summarize the endogenous mechanisms regulating sirtuin activity.
  • To discuss the development of small-molecule compounds that modulate sirtuin activity.

Main Methods:

  • Literature review of sirtuin research.
  • Analysis of biochemical and cellular studies on sirtuin function.
  • Overview of medicinal chemistry efforts for sirtuin modulator discovery.

Main Results:

  • Sirtuins catalyze deacetylation and other deacylation reactions crucial for cellular homeostasis.
  • Endogenous factors and post-translational modifications dynamically control sirtuin activity.
  • Small-molecule modulators are being developed to target specific sirtuins for therapeutic benefit.

Conclusions:

  • Sirtuins are critical regulators of cellular processes with therapeutic potential.
  • A deeper understanding of sirtuin chemistry and regulation is essential for drug development.
  • Targeted modulation of sirtuin activity holds promise for treating diseases associated with aging and metabolic dysfunction.