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Related Concept Videos

Mitochondria01:37

Mitochondria

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Mitochondria are eukaryotic cellular organelles that are known to produce energy through a process called oxidative phosphorylation. Besides their primary function, mitochondria are involved in various cellular processes, including cell growth, differentiation, signaling, metabolism, and senescence. Age-related changes cause a decline in mitochondrial quality and integrity due to increased mitochondrial mutations and oxidative damage. Thus, aging can severely impact mitochondrial functions,...
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Mitochondrial Membranes01:45

Mitochondrial Membranes

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A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...
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Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
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Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

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The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
ROS generation is regulated and maintained at moderate levels necessary...
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The Inner Mitochondrial Membrane01:28

The Inner Mitochondrial Membrane

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The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria.  In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...
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Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

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Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
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Updated: Jun 15, 2025

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
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The Role of Sirtuin-1 Isoforms in Regulating Mitochondrial Function.

Pankaj Patyal1, Fathima S Ameer1, Ambika Verma1

  • 1Donald W. Reynolds Department of Geriatrics and Institute on Aging, University of Arkansas for Medical Sciences, Little Rock, AR 72205, USA.

Current Issues in Molecular Biology
|August 28, 2024
PubMed
Summary

The full-length sirtuin-1 (SIRT1) isoform boosts mitochondrial function and ATP production. Alternatively spliced SIRT1 variants with lost domains show reduced function, impacting cellular metabolism and gene expression.

Keywords:
acetylationbioenergeticsdomain losshistone-H4mitochondriasirtuin-1

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Area of Science:

  • Molecular biology
  • Cellular metabolism
  • Gene regulation

Background:

  • Sirtuin-1 (SIRT1) undergoes alternative splicing, producing isoforms with varying domain structures.
  • The functional consequences of domain loss in SIRT1 isoforms, particularly non-catalytic domains, are not fully understood.
  • Alternative splicing of SIRT1 may influence cellular functions relevant to aging and metabolic diseases.

Purpose of the Study:

  • To compare the function of the full-length SIRT1 isoform (SIRT1-v1) with alternatively spliced isoforms (SIRT1-v2, SIRT1-v3) lacking N-terminal domains.
  • To investigate the impact of SIRT1 isoform structure on mitochondrial respiration and cellular energy production.
  • To determine how domain loss in SIRT1 affects histone acetylation and gene expression of mitochondrial proteins.

Main Methods:

  • Utilized muscle cells and SIRT1-knockout cell lines for functional assays.
  • Compared the activity of SIRT1-v1, SIRT1-v2, and SIRT1-v3 isoforms.
  • Assessed oxidative phosphorylation, ATP production, mitochondrial respiratory complex activity, histone H4 acetylation, and gene expression.

Main Results:

  • Alternatively spliced SIRT1 isoforms (SIRT1-v2, SIRT1-v3) with N-terminal domain loss exhibited attenuated function compared to full-length SIRT1-v1.
  • SIRT1-v1 significantly enhanced oxidative phosphorylation and ATP production rates.
  • SIRT1-v1 specifically upregulated mitochondrial respiratory complex I, altered histone H4 acetylation patterns, and influenced metabolic balance.

Conclusions:

  • Partial loss of N-terminal domains in SIRT1 isoforms impairs their regulatory functions, particularly concerning mitochondrial respiration.
  • The full-length SIRT1 isoform plays a crucial role in optimizing mitochondrial energy production.
  • Age-related increases in alternatively spliced SIRT1 isoforms may have significant implications for mitochondrial health and metabolic regulation, warranting further study.