EXOSC2: A Protein Involved in Inflammation, Fibrosis and Cell Signaling

Target Name: EXOSC2

NCBI ID: G23404

EXOSC2: A Protein Involved in Inflammation, Fibrosis and Cell Signaling

EXOSC2 (SHRF), also known as SFRP2, is a protein that is expressed in various tissues throughout the body, including the brain, heart, and kidneys. It is a member of the superfamily of cytoskeletal proteins, which are involved in the structure and function of cells.

One of the unique features of EXOSC2 is its ability to interact with the protein Fyn, which is known for its role in the immune response and cell signaling. This interaction between EXOSC2 and Fyn has led to the speculation that EXOSC2 may be a drug target or biomarker for various diseases.

EXOSC2 has been shown to play a role in the inflammation of inflammation and fibrosis, which are two of the leading causes of disease and death worldwide. It has been shown to promote the recruitment of immune cells to sites of inflammation and to contribute to the development of fibrosis.

In addition to its role in inflammation and fibrosis, EXOSC2 has also been shown to be involved in the regulation of cell signaling and metabolism. It has been shown to interact with a variety of intracellular signaling pathways, including TGF-β, PI3K, and NF -kappa-B.

EXOSC2 has also been shown to be involved in the regulation of cell adhesion and migration. It has been shown to interact with the protein tight junction protein, known as Zon selfish, which is involved in the regulation of cell adhesion and migration.

In conclusion, EXOSC2 is a protein that has been shown to play a role in a variety of biological processes that are important for human health and disease. Its interaction with Fyn and its role in the regulation of inflammation, fibrosis, and cell signaling warrant further investigation as potential drug targets or biomarkers for various diseases.

Protein Name: Exosome Component 2

Functions: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC2 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC4 and EXOSC7

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