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Related Concept Videos

Caspases01:24

Caspases

Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside cells.
Apoptosis01:30

Apoptosis

Apoptosis is a combination of two Greek words, 'apo' and 'ptosis,' meaning separation and falling off, respectively. Hippocrates used this word to describe gangrene, which was caused due to bandaging of fractured bones. Apoptosis was distinguished from necrosis in 1970 when John Kerr reported observations of morphological changes occurring during apoptosis. During one experiment, he observed that the disruption of blood supply to the liver tissue resulted in a size reduction of the tissue.
The Intrinsic Apoptotic Pathway01:31

The Intrinsic Apoptotic Pathway

Internal cellular stress, such as cellular injury or hypoxia, triggers intrinsic apoptosis. The B-cell lymphoma 2 (Bcl-2) family of proteins are the primary regulators of the intrinsic apoptotic pathway. For example, during DNA damage, checkpoint proteins, such as Ataxia Telangiectasia Mutated (ATM protein) and Checkpoints Factor-2 (Chk2) proteins, are activated. These proteins phosphorylate p53 which further activates pro-apoptotic proteins, such as Bax, Bak, PUMA, and Noxa, and inhibits...
The Extrinsic Apoptotic Pathway01:17

The Extrinsic Apoptotic Pathway

The extrinsic apoptotic pathway is initiated when extracellular death-inducing signals, such as specific cytokines, activate the death receptors expressed on the cell surface. The immune cells involved in this pathway are natural killer cells (NK cells) and cytotoxic T-lymphocytes. NK cells are critical in innate immune response, while cytotoxic T-lymphocytes are associated with adaptive immune response. These cells recognize specific receptors expressed on the altered cells and activate...
Autophagic Cell Death01:18

Autophagic Cell Death

Christian de Duve discovered “autophagy,” a process in which cellular components are engulfed by membrane-bound organelles called autophagosomes. The autophagosomes then fuse with lysosomes to digest the enclosed contents. Autophagy is generally activated in cells to prevent cell death. However, cell death is triggered when the damage is beyond repair.
Autophagy and Apoptosis
Autophagy can activate apoptosis. In normal conditions, the autophagy activating protein Beclin-1 and pro-apoptotic...
Cellular Injury V: Apoptosis and Autophagy01:22

Cellular Injury V: Apoptosis and Autophagy

Cells respond to damage and stress through highly coordinated processes that decide whether they survive or undergo controlled self-destruction. Two major pathways involved in this regulation are apoptosis, a type of programmed cell death, and autophagy, a survival mechanism that helps cells adapt to adverse conditions.ApoptosisApoptosis removes aged or injured cells to maintain tissue balance. During this process, the cell shrinks, chromatin condenses and fragments, and membrane-bound...

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Related Experiment Video

Updated: Jul 14, 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

Cytoplasm-localized SIRT1 enhances apoptosis.

Qihuang Jin1, Tingting Yan, Xinjian Ge

  • 1Institute for Nutritional Sciences, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Graduate School of the Chinese Academy of Sciences, Shanghai, China.

Journal of Cellular Physiology
|May 23, 2007
PubMed
Summary

Sirtuin 1 (SIRT1) can move from the nucleus to the cytoplasm, where it increases cell sensitivity to apoptosis (programmed cell death) independent of its deacetylase function.

More Related Videos

Activation of Apoptosis by Cytoplasmic Microinjection of Cytochrome c
07:42

Activation of Apoptosis by Cytoplasmic Microinjection of Cytochrome c

Published on: June 29, 2011

Related Experiment Videos

Last Updated: Jul 14, 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

Activation of Apoptosis by Cytoplasmic Microinjection of Cytochrome c
07:42

Activation of Apoptosis by Cytoplasmic Microinjection of Cytochrome c

Published on: June 29, 2011

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Sirtuin 1 (SIRT1) is generally known to be a nuclear protein.
  • Its role in cellular processes, particularly apoptosis, is extensively studied.

Purpose of the Study:

  • To investigate the subcellular localization of SIRT1 beyond the nucleus.
  • To determine the functional consequences of cytoplasmic SIRT1 localization on apoptosis.

Main Methods:

  • Immunofluorescence to detect endogenous and exogenous SIRT1 localization.
  • Truncation and fusion protein experiments to manipulate SIRT1 nuclear localization signals.
  • Caspase activity assays to assess apoptosis.
  • Mitotic cell analysis.

Main Results:

  • Endogenous and exogenous SIRT1 were found to partially localize in the cytoplasm in specific cell lines.
  • Cytoplasmic SIRT1 was associated with increased apoptosis sensitivity.
  • Nuclear export of SIRT1 was identified as a key mechanism for its cytoplasmic localization.
  • Cytoplasmic SIRT1 enhanced apoptosis independently of its deacetylase activity but required caspases.
  • SIRT1 accumulated in the cytoplasm during metaphase, augmenting mitotic cell apoptosis.

Conclusions:

  • SIRT1 exhibits cytoplasmic localization, contributing to apoptosis.
  • Cytoplasmic SIRT1 enhances apoptosis through a caspase-dependent pathway, irrespective of its deacetylase activity.
  • The findings reveal a novel role for SIRT1 in regulating apoptosis via its subcellular distribution.