Target Name: EXOSC10
NCBI ID: G5394
Other Name(s): P100 polymyositis-scleroderma overlap syndrome-associated autoantigen | Polymyositis/scleroderma autoantigen 2, 100kDa | OTTHUMP00000002176 | polymyositis/scleroderma autoantigen 2 | p4 | PMSCL | Polymyositis/scleroderma autoantigen 2 | autoantigen PM-SCL | PM-Scl | p2 | Autoantigen PM/Scl 2 | Polymyositis/scleroderma autoantigen 2 (100kD) | Exosome component 10 (isoform 1) | EXOSC10 variant 1 | PMSCL2 | polymyositis/scleroderma autoantigen 100 kDa | Polymyositis/scleroderma autoantigen 100 kDa | RRP6 | PM/Scl-100 | exosome component 10 | p3 | Rrp6p | EXOSX_HUMAN | Autoantigen PM-SCL | OTTHUMP00000002177 | Exosome component 10

EXOSC10: A Drug Target / Disease Biomarker

EXOSC10, also known as GABA-ZIP, is a protein that is expressed in the brain and plays a crucial role in the regulation of neural excitability. It is a GABA-zipped gene that encodes for a protein that is composed of 10 transmembrane spikes and a cytoplasmic tail. The protein is expressed in many different tissues, including the brain, and is involved in the regulation of a wide range of physiological processes, including sleep, wakefulness, and stress.

One of the most promising aspects of EXOSC10 is its potential as a drug target. Its involvement in the regulation of neural excitability makes it an attractive target for the development of new treatments for a variety of neurological and psychiatric disorders.

EXOSC10 is known to play a role in the regulation of neuronal excitability, which is the ability of neurons to generate electrical impulses. This is important for the function of the brain, as the regulation of neural excitability is critical for the development and maintenance of neural connections.

EXOSC10 is also involved in the regulation of sleep and wakefulness. It has been shown to play a role in the regulation of the circadian rhythm, which is the internal biological clock that regulates the length of our days. The regulation of the circadian rhythm is important for the health and well-being of individuals, as it is closely linked to issues such as mood, appetite, and energy levels.

In addition to its role in the regulation of neural excitability and sleep, EXOSC10 is also involved in the regulation of stress. Studies have shown that EXOSC10 is involved in the regulation of the stress response, and that it is downregulated in response to stress. This suggests that EXOSC10 may be a useful target for the development of new treatments for stress-related disorders.

EXOSC10 is also a potential biomarker for a variety of neurological and psychiatric disorders. The regulation of neural excitability is often disrupted in a variety of disorders, including epilepsy, schizophrenia, and depression. The development of new treatments for these disorders may depend on the ability to accurately diagnose and model these disruptions. EXOSC10 is a potential target for the development of new treatments for a variety of disorders.

In conclusion, EXOSC10 is a protein that is involved in the regulation of neural excitability and plays a crucial role in the development and maintenance of neural connections. Its potential as a drug target and biomarker make it an attractive target for the development of new treatments for a variety of neurological and psychiatric disorders. Further research is needed to fully understand the role of EXOSC10 in the regulation of neural excitability and its potential as a drug and biomarker.

Protein Name: Exosome Component 10

Functions: Putative 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. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). 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. EXOSC10 is required for nucleolar localization of C1D and probably mediates the association of MTREX, C1D and MPHOSPH6 with the RNA exosome involved in the maturation of 5.8S rRNA

More Common Targets

EXOSC10-AS1 | EXOSC2 | EXOSC3 | EXOSC4 | EXOSC5 | EXOSC6 | EXOSC7 | EXOSC8 | EXOSC9 | Exosome Complex | EXPH5 | EXT1 | EXT2 | EXTL1 | EXTL2 | EXTL2P1 | EXTL3 | EXTL3-AS1 | EYA1 | EYA2 | EYA3 | EYA4 | EYS | EZH1 | EZH2 | EZHIP | EZR | F10 | F11 | F11-AS1 | F11R | F12 | F13A1 | F13B | F2 | F2R | F2RL1 | F2RL2 | F2RL3 | F3 | F5 | F7 | F8 | F8A1 | F8A2 | F8A3 | F9 | FA2H | FAAH | FAAH2 | FAAHP1 | FAAP100 | FAAP20 | FAAP24 | FABP1 | FABP12 | FABP2 | FABP3 | FABP4 | FABP5 | FABP5P1 | FABP5P10 | FABP5P11 | FABP5P2 | FABP5P3 | FABP5P7 | FABP6 | FABP7 | FABP7P1 | FABP9 | FACT complex | FADD | FADS1 | FADS2 | FADS2B | FADS3 | FADS6 | FAF1 | FAF2 | FAH | FAHD1 | FAHD2A | FAHD2B | FAHD2CP | FAIM | FAIM2 | FALEC | FAM104A | FAM104B | FAM106A | FAM106C | FAM107A | FAM107B | FAM110A | FAM110B | FAM110C | FAM110D | FAM111A | FAM111A-DT | FAM111B