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Translational Regulation01:29

Translational Regulation

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Translational regulation in prokaryotes ensures efficient protein synthesis by controlling ribosome access to mRNA. This regulation is mediated by secondary RNA structures, including translational riboswitches, RNA thermometers, and small RNAs (sRNAs), which respond to intracellular and environmental signals to modulate gene expression.Translational RiboswitchesRiboswitches in the leader region of mRNAs can regulate translation by altering the accessibility of the Shine-Dalgarno (SD) sequence,...
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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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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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siRNA - Small Interfering RNAs02:30

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Small interfering RNAs, or siRNAs, are short regulatory RNA molecules that can silence genes post-transcriptionally, as well as the transcriptional level in some cases. siRNAs are important for protecting cells against viral infections and silencing transposable genetic elements.
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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

Published on: February 27, 2016

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SIRT3: as simple as it seems?

David B Lombard1, Bernadette M M Zwaans

  • 1Department of Pathology and Institute of Gerontology, University of Michigan, Ann Arbor, Mich., USA.

Gerontology
|November 7, 2013
PubMed
Summary
This summary is machine-generated.

Sirtuin 3 (SIRT3) regulates longevity and healthspan by influencing mitochondrial function. Emerging evidence suggests SIRT3 may act indirectly through other regulators, revealing complex communication pathways within cells.

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Last Updated: May 6, 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

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Area of Science:

  • Cellular Biology
  • Aging Research
  • Mitochondrial Function

Background:

  • Conserved pathways regulating longevity offer potential for pharmacologic health and lifespan extension.
  • Sirtuin family members, including mitochondrial sirtuin 3 (SIRT3), are known to extend lifespan in invertebrates and improve mammalian healthspan.
  • SIRT3 directly deacetylates mitochondrial proteins, regulating mitochondrial functions and suppressing age-associated diseases.

Purpose of the Study:

  • To investigate the complex regulatory mechanisms of mitochondrial function by SIRT3.
  • To explore the potential indirect roles of SIRT3 in mitochondrial regulation beyond direct deacetylation.
  • To understand how mitochondrial status is communicated within the cell and to the organism.

Main Methods:

  • Review of recent findings on SIRT3's role in mitochondrial regulation.
  • Analysis of studies investigating SIRT3's interaction with adenosine monophosphate-activated protein kinase (AMPK) and PGC1α.
  • Examination of data from tissue-specific SIRT3 knockout models.

Main Results:

  • SIRT3 promotes the activity of upstream mitochondrial regulators, adenosine monophosphate-activated protein kinase (AMPK) and PGC1α.
  • Evidence suggests SIRT3 may regulate some mitochondrial functions indirectly, not solely through direct deacetylation.
  • Tissue-specific SIRT3 knockouts indicate non-tissue-autonomous roles for SIRT3.

Conclusions:

  • Mitochondrial regulation by SIRT3 is more complex than previously thought, involving both direct and indirect mechanisms.
  • SIRT3's indirect actions may involve signaling pathways that communicate mitochondrial status.
  • Further unraveling these mechanisms could reveal novel insights into cellular and organismal communication regarding mitochondrial health.