EMC4: A Protein Involved in Cellular Processes and Drug Targeting

Target Name: EMC4

NCBI ID: G51234

EMC4

EMC4: A Protein Involved in Cellular Processes and Drug Targeting

EMC4 (Endoplasmic Reticulum-Associated Chaperone 4) is a protein that is expressed in most tissues and is involved in the transport of various molecules throughout the cell. It plays a crucial role in the retrieval of intracellular vesicles, which are small organelles that contain various proteins, including enzymes, toxins, and signaling molecules. EMC4 is also involved in the delivery of exogenous substances, such as viruses and other pathogens, to the cell surface.

EMC4 is a member of the superfamily of chaperones, which are a type of protein that can interact with other proteins to facilitate their interactions and transport. There are several different types of chaperones, including transport chaperones, which transport proteins from one location to another, and effector chaperones, which interact with specific target proteins to regulate their activity. EMC4 is an example of a transport chaperone, as it is involved in the delivery of various molecules to the endoplasmic reticulum, which is the site where proteins are translated from mRNA and then processed and degraded.

EMC4 is composed of 165 amino acid residues and has a calculated molecular weight of 19.9 kDa. It is expressed in most tissues and is involved in the delivery of various vesicles, including intracellular vesicles and exogenous vesicles. EMC4 is also involved in the delivery of viruses and other pathogens to the cell surface.

EMC4 has been shown to play a role in the regulation of cellular processes, including cell signaling, DNA replication, and virus infection. For example, studies have shown that EMC4 can interact with the protein HSP70, which is involved in the detoxification of harmful substances. By interacting with paclitaxel, EMC4 can facilitate the detoxification of these substances and protect the cell from damage.

EMC4 has also been shown to play a role in the regulation of protein function. For example, studies have shown that EMC4 can interact with the protein Co-regulated Carrier Proteins (CCP) to regulate the transport of various proteins to the endoplasmic reticulum. By Interacting with CCPs, EMC4 can influence the strength of these interactions and the rate at which proteins are transported to the endoplasmic reticulum.

In addition to its role in cellular processes, EMC4 has also been shown to be a potential drug target. Studies have shown that EMC4 can be inhibited by small molecules, such as inhibitors of tyrosine phosphorylation. This suggests that EMC4 may be a target for therapeutic intervention in a variety of diseases.

Overall, EMC4 is a protein that is involved in the delivery of various molecules to the endoplasmic reticulum. Its role in cellular processes, including cell signaling and protein function, makes it a potential drug target. Further research is needed to fully understand the mechanisms of EMC4's function and its potential as a therapeutic intervention.

Protein Name: ER Membrane Protein Complex Subunit 4

Functions: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins (PubMed:30415835, PubMed:29809151, PubMed:29242231, PubMed:32459176, PubMed:32439656). Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues (PubMed:30415835, PubMed:29809151, PubMed:29242231). Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices (PubMed:30415835, PubMed:29809151). It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes (PubMed:29809151, PubMed:29242231). By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors (PubMed:30415835). By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes (Probable)

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