Related Experiment Video

Updated: Jul 20, 2026

Detecting Protein Subcellular Localization by Green Fluorescence Protein Tagging and 4',6-Diamidino-2-phenylindole Staining in Caenorhabditis elegans
09:36

Detecting Protein Subcellular Localization by Green Fluorescence Protein Tagging and 4',6-Diamidino-2-phenylindole Staining in Caenorhabditis elegans

Published on: July 30, 2018

Matefin/SUN-1 is a nuclear envelope receptor for CED-4 during Caenorhabditis elegans apoptosis

Yonatan B Tzur1, Ayelet Margalit, Naomi Melamed-Book

  • 1Department of Genetics, Institute of Life Sciences, Hebrew University of Jerusalem, Jerusalem 91904, Israel.

Proceedings of the National Academy of Sciences of the United States of America
|August 30, 2006
PubMed

Insights

The inner nuclear membrane protein matefin/SUN-1 acts as the nuclear envelope receptor for CED-4, facilitating its translocation and maintenance during apoptosis in C. elegans. This discovery links cytoplasmic and nuclear events in programmed cell death.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • The antiapoptotic protein CED-9 in C. elegans sequesters proapoptotic CED-4 at the mitochondria.
  • Apoptosis initiation involves EGL-1 binding CED-9, releasing CED-4 and activating caspase CED-3.

Purpose of the Study:

  • To identify the nuclear envelope (NE) receptor for CED-4.
  • To elucidate the role of this NE receptor in CED-4 translocation and apoptosis execution.

Main Methods:

  • RNA interference (RNAi) for matefin/SUN-1 down-regulation.
  • Analysis of CED-4 translocation to the NE.
  • Quantification of apoptotic cell numbers.

Main Results:

  • Identified matefin/SUN-1 as the NE receptor that binds CED-4.
  • Demonstrated matefin/SUN-1 is essential for CED-4 translocation and NE localization.
  • Observed a significant reduction in apoptotic cells upon matefin/SUN-1 RNAi.

Conclusions:

  • matefin/SUN-1 is the inner nuclear membrane receptor for CED-4.
  • matefin/SUN-1 plays a crucial role in CED-4 localization and the execution of apoptosis.
  • This finding establishes a link between cytoplasmic and nuclear apoptotic pathways.

More Related Videos

A Screenable In Vivo Assay for Mitochondrial Modulators Using Transgenic Bioluminescent Caenorhabditis elegans11:43

A Screenable In Vivo Assay for Mitochondrial Modulators Using Transgenic Bioluminescent Caenorhabditis elegans

Published on: October 16, 2015

Combined Nucleotide and Protein Extractions in Caenorhabditis elegans10:37

Combined Nucleotide and Protein Extractions in Caenorhabditis elegans

Published on: March 17, 2019

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.
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...
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...
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 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...
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR activation may...