Related Experiment Video

Updated: Aug 7, 2026

Silencing of BRCA2 to Identify Novel BRCA2-regulated Biological Functions in Cultured Human Cells
09:24

Silencing of BRCA2 to Identify Novel BRCA2-regulated Biological Functions in Cultured Human Cells

Published on: August 12, 2015

BRD2 is one of BRD7-interacting proteins and its over-expression could initiate apoptosis

Ming Zhou1, Xiao-Jie Xu, Hou-De Zhou

  • 1Cancer Research Institute, Central South University Xiang-Ya School of Medicine, Changsha, Hunan, 410078, China.

Molecular and Cellular Biochemistry
|June 21, 2006
PubMed

Insights

Bromodomain-containing protein 7 (BRD7) interacts with BRD2, a protein implicated in nasopharyngeal carcinoma (NPC). BRD2 localizes to the nucleus and plays a role in initiating cell apoptosis, with a specific nuclear pattern potentially marking this process.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Cancer Research

Background:

  • Bromodomain-containing protein 7 (BRD7) is a potential nuclear transcription regulator linked to nasopharyngeal carcinoma (NPC).
  • BRD2, a potential binding partner of BRD7, was previously identified via a yeast two-hybrid screen.
  • Understanding the interaction between BRD7 and BRD2 is crucial for elucidating their roles in cellular functions and NPC pathogenesis.

Purpose of the Study:

  • To confirm the interaction between BRD7 and BRD2 in mammalian cells.
  • To investigate the subcellular localization of BRD2.
  • To determine the role of BRD2 in cell biology, particularly in initiating apoptosis.

Main Methods:

  • Immunoprecipitation assays to verify BRD7-BRD2 interaction, including truncated BRD2 constructs.
  • Subcellular colocalization studies to assess the spatial relationship between BRD7 and BRD2.
  • GFP fluorescence and Hoechst 33258 staining to analyze BRD2 localization and its effect on apoptosis in COS7 and HNE1 cells.

Main Results:

  • BRD7 directly interacts with BRD2 in mammalian cells.
  • The interaction interface is mapped to amino acids 430–798 of BRD2.
  • BRD2 exhibits nuclear localization with both diffused and dotted patterns, and the dotted pattern correlates with the initiation of apoptosis.

Conclusions:

  • BRD7 and BRD2 form a complex, with a specific region of BRD2 mediating the interaction.
  • BRD2's nuclear localization, particularly its dotted pattern, is associated with the induction of apoptosis.
  • These findings provide insights into the molecular mechanisms underlying BRD2 function and its potential role in NPC.

More Related Videos

Examining BCL-2 Family Function with Large Unilamellar Vesicles08:35

Examining BCL-2 Family Function with Large Unilamellar Vesicles

Published on: October 5, 2012

Related Concept Videos

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...
Negative Regulator Molecules01:23

Negative Regulator Molecules

Positive regulators allow a cell to advance through cell cycle checkpoints. Negative regulators have an equally important role as they terminate a cell’s progression through the cell cycle—or pause it—until the cell meets specific criteria.
Abnormal Proliferation02:23

Abnormal Proliferation

Under normal conditions, most adult cells remain in a non-proliferative state unless stimulated by internal or external factors to replace lost cells. Abnormal cell proliferation is a condition in which the cell's growth exceeds and is uncoordinated with normal cells. In such situations, cell division persists in the same excessive manner even after cessation of the stimuli, leading to persistent tumors. The tumor arises from the damaged cells that replicate to pass the damage to the daughter...
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 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...