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Caspase recruitment domains for protein interactions in cellular signaling (Review)
1Department of Pharmacy, College of Pharmacy, Chung‑Ang University, Seoul 06974, Republic of Korea.
Insights
The caspase recruitment domain (CARD) is key in cell signaling and disease. Structural studies reveal how CARD interactions assemble signaling complexes, improving understanding of cellular processes and diseases like cancer.
Area of Science:
- Molecular Biology
- Structural Biology
- Immunology
Background:
- The caspase recruitment domain (CARD) is a protein interaction module within the death domain (DD) superfamily.
- The DD superfamily is crucial for apoptosis and immune cell signaling.
- CARD interactions are implicated in human diseases such as cancer and neurodegenerative disorders.
Purpose of the Study:
- To review and discuss structural studies of CARDs and their complexes.
- To elucidate the mechanisms governing the assembly and disassembly of CARD-mediated signaling complexes.
- To enhance the understanding of cellular signaling processes involving CARDs.
Main Methods:
- Review of existing structural studies on CARDs.
- Analysis of CARD-CARD interactions (homo-type and hetero-type).
- Examination of CARD complexes involved in signaling.
Main Results:
- Structural insights into various CARDs and their complexes have been summarized.
- Mechanisms controlling the formation and dissolution of signaling complexes are highlighted.
- Understanding of CARD-mediated signaling in disease contexts is improved.
Conclusions:
- Structural studies of CARDs provide critical insights into cellular signaling.
- The CARD domain's role in assembling signaling complexes is essential for biological processes.
- Further research on CARDs can advance therapeutic strategies for associated diseases.
Abstract:
The caspase recruitment domain (CARD), a well‑known protein interaction module, belongs to the death domain (DD) superfamily, which includes DDs, death effector domains, and pyrin domains. The DD superfamily mediates the protein interactions necessary for apoptosis and immune cell signaling pathways. Among these domains, the CARD has been studied extensively as it mediates important cellular signaling events that are associated with various human diseases including cancer, neuro‑degenerative diseases and immune disorders. Homo‑type and hetero‑type CARD‑CARD interactions mediate the formation of large signaling complexes, including caspase‑activating complexes and downstream signaling complexes. The present review summarizes and discusses the results of structural studies of various CARDs and their complexes. These studies shed light on the mechanisms that control the assembly and disassembly of signaling complexes and provide an improved understanding of cellular signaling processes.
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