OSBPL5: A Protein Interacting with Oxysterols and Regulating Cellular Processes

Target Name: OSBPL5

NCBI ID: G114879

OSBPL5

OSBPL5: A Protein Interacting with Oxysterols and Regulating Cellular Processes

OXYSTEROL-BINDING PROTEIN HOMOLOGUE 5 (OSBPL5) is a protein that is expressed in various cell types of the human body, including neurons, muscle cells, and blood vessels. It is a member of the superfamily of transmembrane proteins, which means that it spans the cell membrane and is involved in various cellular processes.

One of the unique features of OSBPL5 is its ability to interact with oxysterols, which are a type of lipid molecule that are found in various cell types. Oxysterols are involved in various cellular processes, including signaling pathways and energy metabolism. OSBPL5 has been shown to play a role in regulating the levels of oxysterols in different cell types, which may have implications for its function in various cellular processes.

OSBPL5 has also been shown to be involved in the regulation of cellular signaling pathways. For example, studies have shown that OSBPL5 can interact with various signaling molecules, including GPRCz, a G protein-coupled receptor that is involved in pain signaling. This interaction between OSBPL5 and GPRCz suggests that OSBPL5 may be a potential drug target or biomarker for pain management.

Another potential function of OSBPL5 is its role in energy metabolism. OSBPL5 has been shown to interact with the protein p53, which is involved in the regulation of DNA damage and repair. This interaction suggests that OSBPL5 may be involved in the regulation of energy metabolism, including the regulation of cell cycle progression and the detoxification of damaged DNA.

OSBPL5 has also been shown to play a role in the regulation of cellular adhesion. Adhesion is the process by which cells stick together to form tissues and organs. OSBPL5 has been shown to interact with the protein cadherin, which is involved in cell-cell adhesion. This interaction suggests that OSBPL5 may be involved in the regulation of cell-cell adhesion, which may have implications for the development of various diseases.

In conclusion, OSBPL5 is a protein that has been shown to interact with various signaling molecules and play a role in the regulation of various cellular processes. Its unique ability to interact with oxysterols and its involvement in the regulation of cellular signaling pathways, energy metabolism, and adhesion suggest that it may be a potential drug target or biomarker for various diseases. Further research is needed to fully understand the function of OSBPL5 in the human body.

Protein Name: Oxysterol Binding Protein Like 5

Functions: Lipid transporter involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane: specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum. Binds phosphatidylserine and PI4P in a mutually exclusive manner (PubMed:23934110, PubMed:26206935). May cooperate with NPC1 to mediate the exit of cholesterol from endosomes/lysosomes (PubMed:21220512). Binds 25-hydroxycholesterol and cholesterol (PubMed:17428193)

The "OSBPL5 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 OSBPL5 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
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•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   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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