CAPNS2: A Calcium-Dependent Protease Subunit 2 as a Drug Target or Biomarker

Target Name: CAPNS2

NCBI ID: G84290

CAPNS2

CAPNS2: A Calcium-Dependent Protease Subunit 2 as a Drug Target or Biomarker

Introduction

CAPNS2, or Calcium-Dependent Protease Small Subunit 2, is a protein that plays a crucial role in the regulation of protein degradation in the endoplasmic reticulum (ER) of eukaryotic cells. It is a member of the family of proteases known as the 尾- proteasome, which are responsible for breaking down various proteins into smaller peptides for recycling or degradation. The activity of CAPNS2 is regulated by the presence of calcium ions, which influence its stability and stability-dependent interactions with other cellular components.

CAPNS2 functions as a negative regulator of the 尾-proteasome, limiting the processing of some target proteins and promoting the processing of others. This process is critical for maintaining the diversity and homeostasis of the cell's proteasome, as well as for ensuring the efficient disposal of damaged or unnecessary proteins. In addition to its role in regulating protein degradation, CAPNS2 is also involved in the regulation of protein synthesis and in modulating cellular signaling pathways.

CAPNS2 is a protein that can be targeted by small molecules, such as drugs, to either inhibit or enhance its activity. As a drug target, CAPNS2 could be used to treat a variety of diseases associated with protein misfolding or degradation, including neurodegenerative disorders, diseases of the immune system, and cancer. In addition, as a biomarker, CAPNS2 levels could be used to monitor the efficacy of therapeutic interventions aimed at modifying the activity of the 尾-proteasome.

The Structure and Functions of CAPNS2

The structure of CAPNS2 is characterized by a unique combination of both protein and nucleic acid domains. It consists of a 156-amino acid protein that is 120 amino acids long and a 26-amino acid RNA molecule that is synthesized from the protein using reverse transcription . The protein consists of a catalytic center, a transmembrane region, and a cytoplasmic tail.

The catalytic center of CAPNS2 is the site of its catalytic activity, where it interacts with various substrate proteins to facilitate the processing of these proteins. The transmembrane region is responsible for the regulation of the activity of the enzyme and serves as a site for its stability . The cytoplasmic tail is involved in the regulation of the protein's stability and in its trafficking to the endoplasmic reticulum.

The activity of CAPNS2 is regulated by the presence of calcium ions. When calcium ions are present, CAPNS2 is fully active and can interact with its substrate proteins to facilitate the processing of these proteins. When calcium ions are not present, CAPNS2 is less active and is not able to support the processing of its substrate proteins. This regulation is critical for maintaining the diversity and homeostasis of the cell's proteasome and for ensuring the efficient disposal of damaged or unnecessary proteins.

CAPNS2 Interactions with Other Cellular Components

CAPNS2 does not exist in isolation in organelles or tissues, but interacts with other organelles and molecules and participates in the regulation of multiple signaling pathways and pathways. First, CAPNS2 can interact with receptors on the cell membrane and mediate the signal transduction process on the cell membrane. Second, CAPNS2 interacts with a variety of intracellular molecules, including neurotransmitter receptors that bind to ceramide. In addition, CAPNS2 also interacts with hydrolases in lysosomes to mediate intracellular degradation processes.

The role of CAPNS2 in tumors has also been well established. Studies have shown that the expression level of CAPNS2 is positively correlated with the prognosis of various cancers, especially in lung and prostate cancers. In addition, the expression level of CAPNS2 is also related to the development of various cancers.

Protein Name: Calpain Small Subunit 2

Functions: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. This small subunit may act as a tissue-specific chaperone of the large subunit, possibly by helping it fold into its correct conformation for activity

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The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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