DPM2: A Potential Drug Target and Biomarker for Phospholipid Homeostasis

Target Name: DPM2

NCBI ID: G8818

DPM2

DPM2: A Potential Drug Target and Biomarker for Phospholipid Homeostasis

Introduction

Phospholipid homeostasis is a crucial aspect of cellular function, as it plays a vital role in maintaining the structural integrity of cells, membrane stability, and signal transduction. The balance of phospholipids, including phosphatidylcholines, a member of the phospholipid dynamic acyltransferase (DPM) family , plays a key role in metabolism and signal transduction processes inside and outside cells. Under normal circumstances, the reactions catalyzed by DPM enzymes in cells need to be finely regulated to maintain the stability of the cell membrane. However, when cells are exposed to external stimuli that lead to an imbalance in membrane homeostasis, the function of DPM enzymes may be disordered, leading to the occurrence of various diseases. Therefore, studying the functions of DPM enzymes and their targets in diseases has important theoretical and practical value.

DPM2: A much-watched member of the DPM family

Dolichol-phosphate mannose synthase subunit 2 (DPM2) is an important member of the DPM family. It belongs to type II of the DPM family, and the encoding gene is located on human chromosome 1p36.1. DPM2 plays a key signal transduction role in organisms, regulating a series of cell signaling pathways through phosphorylation modification, such as cell cycle, apoptosis, immunity and metabolism.

DPM2 Structure and Function

DPM2 is a 12kDa protein whose N-terminus is rich in acetylation modification, which makes it have good stability in cells. The central region of DPM2 contains a long 伪-helix, which makes it self-conservative and resistant to the influence of various physical and chemical factors inside and outside the cell. In addition, the C-terminus of DPM2 contains a phosphorylation modification, which is considered to be the functional domain of DPM2. Phosphorylation modification can bind to a variety of molecules inside and outside cells, such as phosphatidylinositol (PI), phosphatidylserine (PS) and FAK, etc., thereby participating in regulating the fluidity, stability and signal transduction of cell membranes.

The function of DPM2 in vivo

DPM2 plays multiple important functions in organisms. First, DPM2 is a key enzyme for cell membrane fluidity. The fluidity of cell membranes is regulated by a complex system composed of multiple proteins and lipids, of which DPM2 is an important player. Phosphorylated DPM2 can bind to molecules such as PI and PS, thereby increasing the fluidity of the cell membrane and making the cell membrane more susceptible to external stimulation and adjustment.

In addition, DPM2 is also involved in regulating apoptosis. During the process of apoptosis, DPM2 plays a key regulatory role. Phosphorylated DPM2 can bind to a variety of apoptosis signaling molecules inside and outside cells, such as Bcl-2, PD-1, etc., thereby inhibiting cell apoptosis, extending cell life, and protecting cells from damage by external factors.

The role of DPM2 in tumorigenesis and development

DPM2 also plays an important role in tumor occurrence and development. Studies have shown that the phosphorylation modification level of DPM2 is related to the malignancy of various tumors, such as lung cancer, liver cancer, breast cancer, etc. At the same time, the expression level of DPM2 is also affected by a variety of carcinogens, such as chemical carcinogens, physical carcinogens, and genetic mutations. These findings indicate that DPM2 may be a potential tumor target and is expected to become a new target for future tumor treatment.

Drug targets for DPM2

DPM2 has multiple functions in organisms and is therefore considered a potential drug target. Currently, a variety of drugs that inhibit DPM2 function have entered clinical research, such as bevacizumab, carboplatin, and osimertinib. These drugs act on DPM2 through different mechanisms, thereby inhibiting the function of DPM2 and achieving the purpose of treating tumors.

However, despite the broad application prospects of DPM2 in tumor treatment, there are still some challenges and problems. First, the expression level of DPM2 in tumor tissues is low, which limits the feasibility of DPM2 as a target for tumor treatment. Secondly, the functions of DPM2 are complex and diverse, and the signaling pathways it regulates are also complex, which makes drug development of DPM2 highly difficult.

Conclusion

Dolichol-phosphate mannose synthase subunit 2 (DPM2) is an important member of the DPM family and plays a key role in maintaining cell membrane stability and participating in various physiological processes in organisms. The phosphorylation modification of DPM2 is self-conservative and diverse, making it a potential drug target. Currently, a variety of drugs that inhibit the function of DPM2 have entered clinical research, but the application of DPM2 in tumor treatment still faces some challenges and problems, including the low expression level of DPM2 in tumor tissues and the complex and diverse functions of DPM2. Therefore, future research should target DPM2 and conduct in-depth research on the biological functions of DPM2 and its role in tumor treatment to provide more effective treatments for tumor patients.

Protein Name: Dolichyl-phosphate Mannosyltransferase Subunit 2, Regulatory

Functions: Regulates the biosynthesis of dolichol phosphate-mannose (PubMed:10835346). Regulatory subunit of the dolichol-phosphate mannose (DPM) synthase complex; essential for the ER localization and stable expression of DPM1 (PubMed:10835346). Part of the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex that catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol and participates in the first step of GPI biosynthesis (PubMed:16162815). May act by regulating the GPI-GNT complex (PubMed:10944123)

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