Target Name: RNF135
NCBI ID: G84282
Review Report on RNF135 Target / Biomarker Content of Review Report on RNF135 Target / Biomarker
RNF135
Other Name(s): REUL | E3 ubiquitin-protein ligase RNF135 | RING finger protein 135 | RING finger protein leading to RIG-I activation | ring finger protein 135 | Riplet | Ring finger protein 135 | Ring finger protein 135, transcript variant 1 | RIG-I E3 ubiquitin ligase | MMFD | RING-type E3 ubiquitin transferase RNF135 | L13 | RN135_HUMAN | E3 ubiquitin-protein ligase RNF135 (isoform 1) | RNF135 variant 1

RNA-Foldable Neurotransmitter Signaling in the Cell

RNRF135: A Potential Drug Target and Biomarker

Synaptic transmission is a critical aspect of neural network function, and the regulation of neurotransmitter release is at the core of this process. Neurotransmitters, such as dopamine, play a vital role in neural communication, and their release is regulated by a complex cascade of intracellular signaling pathways. One of the key regulators of neurotransmitter release is the RNA-Foldable (RF) protein. In this article, we discuss the role of RF135, a gene that encodes a protein involved in the regulation of neurotransmitter release, as a potential drug target and biomarker for neurological disorders.

The RNA-Foldable gene is a member of the RF family, which includes proteins involved in the regulation of RNA stability and degradation. The RF family is diverse in its functions, with some members involved in the regulation of protein stability, others involved in the regulation of RNA stability, and others involved in the regulation of DNA stability. The RNA-Foldable gene is specifically involved in the regulation of RNA stability, which is critical for the stability and function of RNA-Foldable proteins.

RNA-Foldable proteins are highly conserved, with a conserved C-terminus and a conserved N-terminus that is involved in protein-protein interactions. These proteins can exist in different forms, including soluble, membrane-bound, and nuclear forms. The nuclear The form of RF135 is predominantly localized to the nuclei of cells, where it is involved in the regulation of RNA stability and the stability of RNA-protein interactions.

RNRF135 is a key regulator of neurotransmitter release, and its function in this process is essential for the proper functioning of the nervous system. In neurons, RF135 is involved in the regulation of neurotransmitter release by affecting the stability of the neurotransmitter sigma phosphatidylinositol (SIP) complex. This complex is a critical regulator of neurotransmitter release and is composed of the neurotransmitter receptor, SIP protein, and the protein kinase CK27.

SIP is a transmembrane protein that plays a critical role in the regulation of neurotransmitter release. It is involved in the formation of the SIP-receptor complex, which is responsible for the regulation of neurotransmitter release. receptor, SIP protein, and the protein kinase CK27. CK27 is a key regulator of the SIP-receptor complex, and its function in this process is to phospholylate the SIP protein, which in turn affects the stability of the SIP-receptor complex.

In addition to its role in the regulation of SIP stability, RF135 is also involved in the regulation of the stability of other RNA-Foldable proteins. For example, RF135 is involved in the regulation of the stability of the RNA-protein interaction between the neurotransmitter receptor and the protein kinase CK27. This interaction is critical for the regulation of neurotransmitter release and is a key component of the SIP-receptor complex.

The role of RF135 in the regulation of neurotransmitter release is important for the proper functioning of the nervous system. Disruptions in RF135 function have been implicated in a number of neurological disorders, including neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease.

As a potential drug target, RF135 is a promising target for the development of new therapies for a variety of neurological disorders. For example, drugs that

Protein Name: Ring Finger Protein 135

Functions: E2-dependent E3 ubiquitin-protein ligase that functions as a RIGI coreceptor in the sensing of viral RNAs in cell cytoplasm and the activation of the antiviral innate immune response (PubMed:19017631, PubMed:19484123, PubMed:21147464, PubMed:23950712, PubMed:28469175, PubMed:31006531). Together with the UBE2D3, UBE2N and UB2V1 E2 ligases, catalyzes the 'Lys-63'-linked polyubiquitination of RIGI oligomerized on viral RNAs, an essential step in the activation of the RIG-I signaling pathway (PubMed:19017631, PubMed:21147464, PubMed:28469175, PubMed:31006531). Through a ubiquitin-independent parallel mechanism, which consists in bridging RIGI filaments forming on longer viral RNAs, further activates the RIG-I signaling pathway (PubMed:31006531). This second mechanism that synergizes with the ubiquitin-dependent one would thereby allow an RNA length-dependent regulation of the RIG-I signaling pathway (Probable). Associated with the E2 ligase UBE2N, also constitutively synthesizes unanchored 'Lys-63'-linked polyubiquitin chains that may also activate the RIG-I signaling pathway (PubMed:28469175, PubMed:31006531)

The "RNF135 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 RNF135 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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