TMED10: A Potential Drug Target and Biomarker for Membrane Transport-related Disorders

Target Name: TMED10

NCBI ID: G10972

TMED10

TMED10: A Potential Drug Target and Biomarker for Membrane Transport-related Disorders

Introduction

Membrane transport-related disorders have been a topic of interest in the scientific community for several decades due to their significant impact on various physiological processes. These disorders have been associated with various diseases, including parking syndrome, periodic paralysis, and several others Currently. , there are limited treatment options available for these disorders, which have a significant impact on the quality of life of patients. TMED10, a transmembrane protein identified by researchers, has the potential to be a drug target and biomarker for membrane transport-related disorders.

TMED10: Structure and Function

TMED10 is a protein that belongs to the subfamily of transmembrane proteins, which are involved in the regulation of cellular processes such as ion and solute transport. TMED10 is characterized by the presence of a transmembrane domain and an extracellular domain. The transmembrane domain is responsible for the protein's membrane-spanning properties, while the extracellular domain is involved in its cytoskeletal organization and interaction with other cellular components.

TMED10 has been shown to play a significant role in the regulation of sodium and potassium transport in various organisms, including mammals. Studies have shown that TMED10 is involved in the regulation of the activity of several ion channels, including the Na+/K+-ATPase. This protein is known to play a critical role in the regulation of resting membrane potential (RMP) and can affect the activity of several membrane transport proteins, including Na+/K+-ATPase.

TMED10 as a Drug Target

The potential use of TMED10 as a drug target is based on its involvement in the regulation of membrane transport processes. Several studies have shown that TMED10 can be targeted by small molecules, including inhibitors of the Na+/K+-ATPase. These inhibitors have been shown to block the activity of TMED10 and to reduce the regulation of sodium and potassium transport.

In addition to its potential as a drug target, TMED10 has also been shown to be a potential biomarker for several membrane transport disorders. The regulation of membrane transport processes is known to play a critical role in the development and progression of several diseases, including parking syndrome, periodic paralysis, and several others. Therefore, the regulation of membrane transport processes may be a useful indicator of the severity of these disorders.

TMED10 as a Biomarker

TMED10 has been shown to be involved in the regulation of several membrane transport processes, including the regulation of sodium and potassium transport. This suggests that it may be a useful biomarker for several membrane transport disorders. Several studies have shown that TMED10 levels are affected by several membrane transport disorders, including parking syndrome and periodic paralysis.

In addition to its potential as a drug target, TMED10 has also been shown to be a potential biomarker for several other membrane transport disorders. For instance, studies have shown that TMED10 levels are affected by the severity of periodontal disease, a common inflammatory disorder that is associated with the regulation of membrane transport processes.

Conclusion

TMED10 is a transmembrane protein that has been shown to play a significant role in the regulation of membrane transport processes in various organisms. Its potential as a drug target and biomarker for membrane transport-related disorders makes it an attractive target for future research. Further studies are needed to fully understand the role of TMED10 in the regulation of membrane transport processes and its potential as a drug

Protein Name: Transmembrane P24 Trafficking Protein 10

Functions: Cargo receptor involved in protein vesicular trafficking and quality control in the endoplasmic reticulum (ER) and Golgi (PubMed:10052452, PubMed:11726511, PubMed:16641999, PubMed:17288597, PubMed:19296914, PubMed:20427317, PubMed:21219331, PubMed:27569046). The p24 protein family is a group of transmembrane proteins that bind coat protein complex I/COPI and coat protein complex II/COPII involved in vesicular trafficking between the membranes (PubMed:10052452). Acts at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and involved in vesicle coat formation at the cytoplasmic side (PubMed:20427317, PubMed:27569046). Mainly functions in the early secretory pathway and cycles between the ER, ER-Golgi intermediate compartment (ERGIC) and Golgi, mediating cargo transport through COPI and COPII-coated vesicles (PubMed:10052452, PubMed:10852829, PubMed:12237308). In COPII vesicle-mediated anterograde transport, involved in the transport of GPI-anchored proteins by acting together with TMED2 as their cargo receptor; the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipid raft-like microdomains of the ER (PubMed:20427317, PubMed:27569046). Recognizes GPI anchors structural remodeled in the ER by the GPI inositol-deacylase/PGAP1 and the metallophosphoesterase MPPE1/PGAP5 (By similarity). In COPI vesicle-mediated retrograde transport, involved in the biogenesis of COPI vesicles and vesicle coat recruitment (PubMed:11726511). Involved in trafficking of amyloid beta A4 protein and soluble APP-beta release (independent from the modulation of gamma-secretase activity) (PubMed:17288597). Involved in the KDELR2-mediated retrograde transport of the toxin A subunit (CTX-A-K63)together with COPI and the COOH terminus of KDELR2 (By similarity). On Golgi membranes, acts as primary receptor for ARF1-GDP, a GTP-binding protein involved in COPI-vesicle formation (PubMed:11726511). Increases coatomer-dependent GTPase-activating activity of ARFGAP2 which mediates the hydrolysis of ARF1-bound GTP and therefore modulates protein trafficking from the Golgi apparatus (PubMed:19296914). Involved in the exocytic trafficking of G protein-coupled receptors F2LR1/PAR2 (trypsin and tryspin-like enzyme receptor), OPRM1 (opioid receptor) and P2RY4 (UTD and UDP receptor) from the Golgi to the plasma membrane, thus contributing to receptor resensitization (PubMed:21219331). In addition to its cargo receptor activity, may also act as a protein channel after oligomerization, facilitating the post-translational entry of leaderless cytoplasmic cargo into the ERGIC (PubMed:32272059). Involved in the translocation into ERGIC, the vesicle entry and the secretion of leaderless cargos (lacking the secretion signal sequence), including the mature form of interleukin 1/IL-1 family members, the alpha-crystallin B chain HSPB5, the carbohydrate-binding proteins galectin-1/LGALS1 and galectin-3/LGALS3, the microtubule-associated protein Tau/MAPT, and the annexin A1/ANXA1; the translocation process is dependent on cargo protein unfolding and enhanced by chaperones HSP90AB1 and HSP90B1/GRP9 (PubMed:32272059). Could also associates with the presenilin-dependent gamma-secretase complex in order to regulate gamma-cleavages of the amyloid beta A4 protein to yield amyloid-beta 40/Abeta40 (PubMed:16641999)

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•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
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•   the target screening and validation;
•   expression level;
•   disease relevance;
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•   related combination drugs;
•   pharmacochemistry experiments;
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•   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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