DYRK2: A Potential Drug Target and Biomarker for Multiple Myeloma

Target Name: DYRK2

NCBI ID: G8445

DYRK2

Other Name(s): DYRK2 variant 1 | Dual specificity tyrosine phosphorylation regulated kinase 2, transcript variant 1 | dual specificity tyrosine phosphorylation regulated kinase 2 | Dual specificity tyrosine-phosphorylation-regulated kinase 2 (isoform 1) | Dual specificity tyrosine-phosphorylation-regulated kinase 2 | dual specificity tyrosine-(Y)-phosphorylation regulated kinase 2 | DYRK2_HUMAN

DYRK2: A Potential Drug Target and Biomarker for Multiple Myeloma

Introduction

Multiple myeloma is a type of cancer that originates from a plasma cell, a type of white blood cell that produces antibodies. This cancer is characterized by the production of multiple clone populations of abnormal B cells, leading to the formation of multiple Plasma cell population. DYRK2, a gene that encodes a protein involved in the regulation of mitochondrial fusion, has been identified as a potential drug target and biomarker for multiple myeloma.

DYRK2 and Mitochondrial Fusion

The DYRK2 gene encodes a protein that is involved in the regulation of mitochondrial fusion. Mitochondrial fusion is the process by which one mitochondrion fuses with another, resulting in the formation of a single mitochondrial organ. This process is critical for the survival of the cell, as mitochondria are responsible for generating the majority of the cell's energy.

DYRK2 plays a crucial role in regulating mitochondrial fusion by ensuring that it occurs in a timely and efficient manner. Studies have found that the deletion of DYRK2 protein leads to a decrease in the expression level of DYRK2 gene in the mouse spleen, while significantly inhibiting the expression of mouse B cells. Proliferation and differentiation. In addition, knockdown of the DYRK2 gene also resulted in a reduction in the number of monoclonal plasma cells in the immune organs of mice, further confirming the important role of DYRK2 in regulating B cell proliferation and differentiation.

DYRK2 as a Potential Drug Target

Abnormal expression of DYRK2 is associated with the occurrence of various diseases, including cancer. Studies have shown that knockdown of the DYRK2 gene is positively correlated with the incidence of various cancers, including lung cancer, liver cancer, breast cancer, etc. In addition, knockdown of DYRK2 gene is also associated with chemotherapy resistance and poor treatment response in various cancers. Therefore, DYRK2 has become a potential drug target.

DYRK2-targeted treatment strategies mainly focus on inhibiting the expression of DYRK2 gene and promoting its degradation. Currently, some drugs that inhibit DYRK2 gene expression have entered clinical research, but the mechanism of action of these drugs on DYRK2 is still not completely clear. Therefore, the role of DYRK2 in drug screening and mechanism of action needs to be further studied in the future to guide clinical practice.

DYRK2 as a Biomarker

Detection of DYRK2 gene expression levels is another method to evaluate DYRK2 as a potential drug target. Studies have shown that reduced DYRK2 gene expression levels are a common feature of various cancers, and this reduction is positively correlated with disease progression and invasiveness. Therefore, by detecting DYRK2 gene expression levels, the role of DYRK2 in various cancers can be evaluated and biomarkers can be provided for disease diagnosis and treatment.

in conclusion

The protein encoded by the DYRK2 gene plays an important role in regulating mitochondrial fusion. Abnormal expression of DYRK2 is related to the occurrence of various cancers. Therefore, DYRK2 is a potential drug target. In addition, reduced DYRK2 gene expression levels are a common feature of various cancers and can be used as a biomarker of the disease. Therefore, the role of DYRK2 in drug screening and mechanism of action needs to be further studied in the future to guide clinical practice.

Protein Name: Dual Specificity Tyrosine Phosphorylation Regulated Kinase 2

Functions: Serine/threonine-protein kinase involved in the regulation of the mitotic cell cycle, cell proliferation, apoptosis, organization of the cytoskeleton and neurite outgrowth. Functions in part via its role in ubiquitin-dependent proteasomal protein degradation. Functions downstream of ATM and phosphorylates p53/TP53 at 'Ser-46', and thereby contributes to the induction of apoptosis in response to DNA damage. Phosphorylates NFATC1, and thereby inhibits its accumulation in the nucleus and its transcription factor activity. Phosphorylates EIF2B5 at 'Ser-544', enabling its subsequent phosphorylation and inhibition by GSK3B. Likewise, phosphorylation of NFATC1, CRMP2/DPYSL2 and CRMP4/DPYSL3 promotes their subsequent phosphorylation by GSK3B. May play a general role in the priming of GSK3 substrates. Inactivates GYS1 by phosphorylation at 'Ser-641', and potentially also a second phosphorylation site, thus regulating glycogen synthesis. Mediates EDVP E3 ligase complex formation and is required for the phosphorylation and subsequent degradation of KATNA1. Phosphorylates TERT at 'Ser-457', promoting TERT ubiquitination by the EDVP complex. Phosphorylates SIAH2, and thereby increases its ubiquitin ligase activity. Promotes the proteasomal degradation of MYC and JUN, and thereby regulates progress through the mitotic cell cycle and cell proliferation. Promotes proteasomal degradation of GLI2 and GLI3, and thereby plays a role in smoothened and sonic hedgehog signaling. Plays a role in cytoskeleton organization and neurite outgrowth via its phosphorylation of DCX and DPYSL2. Phosphorylates CRMP2/DPYSL2, CRMP4/DPYSL3, DCX, EIF2B5, EIF4EBP1, GLI2, GLI3, GYS1, JUN, MDM2, MYC, NFATC1, p53/TP53, TAU/MAPT and KATNA1. Can phosphorylate histone H1, histone H3 and histone H2B (in vitro). Can phosphorylate CARHSP1 (in vitro)

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