Target Name: CHMP2B
NCBI ID: G25978
Review Report on CHMP2B Target / Biomarker Content of Review Report on CHMP2B Target / Biomarker
CHMP2B
Other Name(s): Vacuolar protein sorting-associated protein 2-2 | DMT1 | hVps2-2 | ALS17 | Charged multivesicular body protein 2b (isoform 1) | CHM2B_HUMAN | CGI-84 protein | vacuolar protein-sorting-associated protein 2-2 | charged multivesicular body protein 2B | VPS2-2 | CHMP2.5 | VPS2B | Charged multivesicular body protein 2B, transcript variant 1 | CHMP2b | VPS2 homolog B | CHMP2B variant 1 | Vps2-2 | Charged multivesicular body protein 2b | chromatin modifying protein 2B | Chromatin-modifying protein 2b | FTDALS7

CHMP2B: A Potential Drug Target and Biomarker

CHMP2B (Vacuolar protein sorting-associated protein 2-2) is a protein that plays a crucial role in the regulation of protein trafficking in eukaryotic cells. It is a member of the transmembrane protein family, which includes proteins involved in various cellular processes such as signaling, ion transport, and apposporation. CHMP2B is known to function as a negative regulator of the trafficking of its own protein, p120-associated nuclear protein (PAN), which is involved in the intracellular distribution of various cellular proteins.

The CHMP2B gene was first identified in the genomic sequence database as a gene that was highly conserved across various species, including humans. It is located on chromosome 11q22 and has a molecular weight of approximately 42 kDa. CHMP2B is a single gene homologue, which means that it is a copy of the same gene in each cell of the organism.

Expression and Localization

CHMP2B is highly expressed in most tissues of the body, including the brain, heart, and liver. It is predominantly expressed in the endoplasmic reticulum (ER), which is the protein synthesis and quality control organelle that retrieves synthesized proteins from the cytoplasm and delivers them to their final destinations, such as the plasma membrane or various organelles. CHMP2B is also expressed in the nuclear envelope, which is the outermost layer of the nuclear membrane and functions as a barrier to the import of unauthorized proteins into the cell.

CHMP2B is predominantly localized to the endoplasmic reticulum, where it functions as a negative regulator of protein trafficking. It is well established that the endoplasmic reticulum is the primary site of protein synthesis and quality control, and as such, it is the first destination for newly synthesized proteins. However, the import of these proteins into the various organelles and the cell surface is a highly regulated process that is tightly controlled by various proteinases and transmembrane proteins.

CHMP2B plays a crucial role in the regulation of protein import into the ER by interacting with the transmembrane protein known as TAP (Transmembrane Association Protein). TAP is a family of proteins that play a central role in the regulation of protein import and export, including the regulation of vesicular traffic, which is the movement of proteins and other molecules across the endoplasmic reticulum membrane.

CHMP2B functions as a negative regulator of TAP by binding to its extracellular domain and preventing it from interacting with the TAP protein on the endoplasmic reticulum. This interaction between CHMP2B and TAP is critical for the regulation of protein import and export, and is a key step in the process of protein synthesis and quality control.

Drug Target and Biomarker

The regulation of protein import into the ER by TAP and CHMP2B is a critical process that is involved in the regulation of various cellular processes, including cell growth, apoptosis, and inflammation. It is therefore an attractive target for drug development, with potential therapeutic applications in various diseases.

One of the potential drug targets for CHMP2B is the inhibition of its interaction with TAP, which would result in the inhibition of protein import and export. This would result in the accumulation of unprocessed proteins in the ER, which could lead to the formation of aggregates and the disruption of cellular structures and processes, including the regulation of cell growth, apoptosis, and inflammation.

Another potential biomarker for CHMP2B is its expression level, which could be used as a readout for the efficacy of a potential drug. For example, if an drug is able to inhibit the interaction between CHMP2B and TAP, it should result in a decrease in the expression level of CHMP2B, which could be used as a biomarker for the drug's efficacy.

Conclusion

CHMP2B is a protein that plays a crucial role in the regulation of protein trafficking in eukaryotic cells. Its localization to the endoplasmic reticulum and its interaction with TAP are key factors in the regulation of protein import and export, and as such, it is an attractive target for drug development. The inhibition of CHMP2B's interaction with TAP has the potential to therapeutic applications in various diseases, including cancer, neurodegenerative diseases, and autoimmune diseases. Additionally, the regulation of CHMP2B's expression level could be used as a biomarker for the efficacy of a potential drug.

Protein Name: Charged Multivesicular Body Protein 2B

Functions: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4

The "CHMP2B Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about CHMP2B comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
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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