Target Name: RNF103-CHMP3
NCBI ID: G100526767
Other Name(s): RNF103-VPS24 | CGI149 | CHMP3 | RNF103-VPS24 readthrough | VPS24 | Charged multivesicular body protein 3 | RNF103-CHMP3 read-through | RNF103-CHMP3 protein | hVps24 | Neuroendocrine differentiation factor | NEDF | RNF103-CHMP3 readthrough | Chromatin-modifying protein 3 | CHMP3_HUMAN | Vacuolar protein sorting-associated protein 24

RNF103-CHMP3: A Drug Target / Disease Biomarker

RNA-Nucleic Acid-Protein 103 (RNF103) is a protein that is expressed in various cell types of the human body. It is a key regulator of cell proliferation and has been implicated in the development and progression of various diseases. One of the unique features of RNF103 is its ability to interact with the protein CHMP3, which has been shown to play a crucial role in regulating cell signaling pathways.

The CHMP3 protein is a nucleic acid-protein hybrid that is composed of a cytoplasmic domain, a transmembrane domain, and an extracellular domain. It is expressed in various cell types of the human body, including muscle, nerve, and epithelial cells. CHMP3 functions as a negative regulator of several signaling pathways, including the TGF-β pathway.

The TGF-β pathway is a well-established signaling pathway that is involved in various cellular processes, including cell growth, differentiation, and inflammation. It is a critical pathway that regulates the development and maintenance of tissues and organs, and is often dysregulated in various diseases, including cancer.

CHMP3 has been shown to play a crucial role in regulating the TGF-β pathway. It interacts with the cytoplasmic domain of RNF103 and prevents it from activating the TGF-β pathway. This interaction between CHMP3 and RNF103 provides a negative feedback mechanism that helps to maintain the balance of the TGF-β pathway.

In addition to its role in regulating the TGF-β pathway, CHMP3 has also been shown to interact with several other proteins and molecules. It has been shown to interact with the protein FBN1, which is a protein that is involved in the regulation of cell adhesion and migration. It has also been shown to interact with the protein PDGFR-尾, which is a tyrosine kinase that is involved in the regulation of cell signaling pathways.

The identification of RNA-Nucleic Acid-Protein (RNP) interactions is an important area of research, as these interactions can provide new insights into the regulation of cellular processes. The interaction between CHMP3 and RNF103 is an example of a RNP interaction that can have a significant impact on cellular processes.

In conclusion, RNF103 is a protein that is expressed in various cell types of the human body and has been implicated in the development and progression of various diseases. The interaction between RNF103 and the protein CHMP3 is a crucial component of this protein's function. The regulation of the TGF-β pathway by CHMP3 provides a negative feedback mechanism that helps to maintain the balance of this pathway. Further research is needed to fully understand the role of CHMP3 in the regulation of cellular processes and the development of various diseases.

Protein Name: RNF103-CHMP3 Readthrough

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. Selectively binds to phosphatidylinositol 3,5-bisphosphate PtdIns(3,5)P2 and PtdIns(3,4)P2 in preference to other phosphoinositides tested. Involved in late stages of cytokinesis. Plays a role in endosomal sorting/trafficking of EGF receptor. Isoform 2 prevents stress-mediated cell death and accumulation of reactive oxygen species when expressed in yeast cells

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