Unique Protein: UBL4A's Role in G-Coupled Receptor Signaling (G8266)

Target Name: UBL4A

NCBI ID: G8266

Unique Protein: UBL4A's Role in G-Coupled Receptor Signaling

UBL4A (Unique Binding Logic 4.0, GET5) is a protein that is expressed in various tissues of the human body, including the brain, heart, and kidneys. It is a member of the superfamily of nucleotide-binding proteins (NBP), which are a group of proteins that interact with DNA in various ways. UBL4A is unique among NBP proteins because of its specificity for DNA-binding proteins called G-coupled receptors.

G-coupled receptors are a family of transmembrane proteins that play a crucial role in cellular signaling. They are characterized by the presence of a catalytic active site on the intracellular portion of the receptor, which is usually a G protein-coupled receptor. These receptors are involved in a wide range of physiological processes, including sensory perception, neurotransmission, and hormone signaling.

UBL4A is specifically designed to interact with G-coupled receptors. It contains a nucleotide-binding domain (NBD) that is responsible for this interaction. The NBD is composed of a nucleotide-binding core and a nucleotide-binding loop. The nucleotide-binding loop is the part of the NBD that interacts with the G-coupled receptor, while the nucleotide-binding core is responsible for organizing the other components of the protein.

The G-coupled receptor is a transmembrane protein that consists of an extracellular portion and an intracellular portion. The extracellular portion of the receptor is involved in cell-extending processes, while the intracellular portion contains the catalytic active site. UBL4A is designed to interact with the intracellular portion of the G-coupled receptor, where the catalytic active site is located.

The role of UBL4A in G-coupled receptor signaling is not well understood, but it is believed to play a negative regulatory role. UBL4A is known to interact with multiple G-coupled receptors, including GABA receptors, which are involved in anxiety, depression, and other neurological disorders. It is also thought to interact with ion channels, including the calcium ion channels, which are involved in muscle contraction and other physiological processes.

In addition to its role in G-coupled receptor signaling, UBL4A is also involved in the regulation of cellular processes that are important for tissue repair and regeneration. It has been shown to play a role in the regulation of cell proliferation, cell migration, and tissue repair.

UBL4A is also of interest as a potential drug target. Because it is involved in the regulation of G-coupled receptor signaling, it is a potential target for small molecules that can modulate this signaling pathway. This has led to the development of a new class of drugs called G-coupled receptor antagonists, which are designed to inhibit UBL4A's interaction with G-coupled receptors. These drugs have been shown to be effective in treating a variety of neurological and psychiatric disorders, including anxiety, depression, and psychosis.

In conclusion, UBL4A is a unique protein that is involved in the regulation of G-coupled receptor signaling and the regulation of cellular processes important for tissue repair and regeneration. Its specificity for G-coupled receptors makes it a potential drug target, and its role in the regulation of these processes makes it an important molecule for study. Further research is needed to fully understand the function of UBL4A and its potential as a drug target.

Protein Name: Ubiquitin Like 4A

Functions: As part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, maintains misfolded and hydrophobic patches-containing proteins in a soluble state and participates in their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation (PubMed:20676083, PubMed:21636303, PubMed:21743475, PubMed:28104892). The BAG6/BAT3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Recruited to ribosomes, it interacts with the transmembrane region of newly synthesized tail-anchored proteins and together with SGTA and ASNA1 mediates their delivery to the endoplasmic reticulum (PubMed:20676083, PubMed:28104892, PubMed:25535373). Client proteins that cannot be properly delivered to the endoplasmic reticulum are ubiquitinated and sorted to the proteasome (PubMed:28104892). Similarly, the BAG6/BAT3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum (PubMed:21743475). The BAG6/BAT3 complex also plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome (PubMed:21636303)

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