SYK: A Potential Drug Target and Biomarker for Diseases (G6850)

Target Name: SYK

NCBI ID: G6850

Content of Review Report on SYK Target / Biomarker

SYK

SYK: A Potential Drug Target and Biomarker for Diseases

SYK (short for Src-YFU Repeat), a 21-kDa transmembrane protein, has been identified as a potential drug target and biomarker for various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. Its unique structure, which consists of a nucleotide-binding oligomerization (NBO) domain and a coiled-coil region, has led to a high degree of structural flexibility and diverse functions.

SYK has been shown to play a critical role in various cellular processes, including cell signaling, DNA replication, and stress response. Its NBO domain, which consists of a nucleotide-binding oligomerization (NBO) domain and a coiled-coil region, is responsible for the protein's stability and interactions with other cellular components. The NBO domain has been shown to interact with various protein partners, including histone modifications, non-histone modifications, and nucleic acids.

One of the unique features of SYK is its ability to form multiple copies of its NBO domain. This is accomplished through a process called NBO-mediated dimerization, in which two NBO domains can interact with each other and form a dimer. Thisdimerization allows for the formation of a more stable and active protein, as well as the formation of different conformational variants of the protein.

SYK has been shown to play a role in various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. For example, studies have shown that high levels of SYK are associated with poor prognosis in neuroblastoma, a type of cancer that affects children, as well as with the development of neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease. Additionally, SYK has been shown to be involved in the development and progression of autoimmune disorders, such as rheumatoid arthritis and multiple sclerosis.

SYK has also been shown to be a potential drug target. Its unique structure and diverse functions make it an attractive target for small molecules and antibodies that can modulate its activity. Several companies have already filed patents for SYK-targeted compounds, which have the potential to treat various diseases.

In addition to its potential as a drug target, SYK has also been shown to be a potential biomarker. Its unique structure and diverse functions make it an attractive target for diagnostic assays, such as mass spectrometry-based assays and affinity purification experiments. Several studies have shown that SYK-targeted antibodies have the potential to detect and monitor various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

In conclusion, SYK is a unique and highly-studied protein that has the potential to be a drug target and biomarker for various diseases. Its unique structure and diverse functions make it an attractive target for small molecules and antibodies that can modulate its activity. As research continues to advance, its potential as a drug and biomarker will be further defined.

Protein Name: Spleen Associated Tyrosine Kinase

Functions: Non-receptor tyrosine kinase which mediates signal transduction downstream of a variety of transmembrane receptors including classical immunoreceptors like the B-cell receptor (BCR). Regulates several biological processes including innate and adaptive immunity, cell adhesion, osteoclast maturation, platelet activation and vascular development (PubMed:33782605). Assembles into signaling complexes with activated receptors at the plasma membrane via interaction between its SH2 domains and the receptor tyrosine-phosphorylated ITAM domains. The association with the receptor can also be indirect and mediated by adapter proteins containing ITAM or partial hemITAM domains. The phosphorylation of the ITAM domains is generally mediated by SRC subfamily kinases upon engagement of the receptor. More rarely signal transduction via SYK could be ITAM-independent. Direct downstream effectors phosphorylated by SYK include VAV1, PLCG1, PI-3-kinase, LCP2 and BLNK. Initially identified as essential in B-cell receptor (BCR) signaling, it is necessary for the maturation of B-cells most probably at the pro-B to pre-B transition. Activated upon BCR engagement, it phosphorylates and activates BLNK an adapter linking the activated BCR to downstream signaling adapters and effectors. It also phosphorylates and activates PLCG1 and the PKC signaling pathway. It also phosphorylates BTK and regulates its activity in B-cell antigen receptor (BCR)-coupled signaling. In addition to its function downstream of BCR also plays a role in T-cell receptor signaling. Plays also a crucial role in the innate immune response to fungal, bacterial and viral pathogens. It is for instance activated by the membrane lectin CLEC7A. Upon stimulation by fungal proteins, CLEC7A together with SYK activates immune cells inducing the production of ROS. Also activates the inflammasome and NF-kappa-B-mediated transcription of chemokines and cytokines in presence of pathogens. Regulates neutrophil degranulation and phagocytosis through activation of the MAPK signaling cascade (By similarity). Required for the stimulation of neutrophil phagocytosis by IL15 (PubMed:15123770). Also mediates the activation of dendritic cells by cell necrosis stimuli. Also involved in mast cells activation. Involved in interleukin-3/IL3-mediated signaling pathway in basophils (By similarity). Also functions downstream of receptors mediating cell adhesion. Relays for instance, integrin-mediated neutrophils and macrophages activation and P-selectin receptor/SELPG-mediated recruitment of leukocytes to inflammatory loci. Also plays a role in non-immune processes. It is for instance involved in vascular development where it may regulate blood and lymphatic vascular separation. It is also required for osteoclast development and function. Functions in the activation of platelets by collagen, mediating PLCG2 phosphorylation and activation. May be coupled to the collagen receptor by the ITAM domain-containing FCER1G. Also activated by the membrane lectin CLEC1B that is required for activation of platelets by PDPN/podoplanin. Involved in platelet adhesion being activated by ITGB3 engaged by fibrinogen. Together with CEACAM20, enhances production of the cytokine CXCL8/IL-8 via the NFKB pathway and may thus have a role in the intestinal immune response (By similarity)

The "SYK Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about SYK comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   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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