SACM1L: A Potential Drug Target and Biomarker for Phosphatidylinositol-3-Phosphatase

Target Name: SACM1L

NCBI ID: G22908

SACM1L

SACM1L: A Potential Drug Target and Biomarker for Phosphatidylinositol-3-Phosphatase

Phosphatidylinositol-3-phosphatase (PIP3) is a protein that plays a crucial role in cellular signaling and memory. It is a key enzyme in the PI3K/Akt signaling pathway, which regulates various cellular processes including cell growth, differentiation, and survival. SACM1L (phosphatidylinositol-3-phosphatase SAC1, isoform 1) is an enzyme that catalyzes the breakdown of phosphatidylinositol-3-phosphate (PIP3) to generate phosphatidylinositol (PI) and inositol, which are crucial for the formation of various signaling pathways.

SACM1L is an attractive drug target due to its unique structure and its involvement in cellular signaling. It is a single-chain protein with 114 amino acid residues and 19% amino acid acidity. It has a catalytic active site that is highly conserved and is known to have a unique catalytic triad. The catalytic triad consists of the amino acids Asp-212, Asn-213, and Asp-214, which are crucial for the stability and activity of the enzyme.

SACM1L functions as a negative regulator of the PI3K/Akt signaling pathway. It inhibits the phosphorylation of the protein p110, which is a key regulator of the PI3K pathway. The inhibition of p110 phosphorylation by SACM1L leads to the inhibition of downstream signaling pathways, including the regulation of cell growth, differentiation, and survival.

SACM1L is also a potent inhibitor of the PI3K/Akt signaling pathway in cancer cells. In cancer cells, the PI3K/Akt signaling pathway is often overexpressed, leading to the formation of uncontrolled cell growth and the development of cancer. SACM1L has been shown to inhibit the growth and survival of various cancer cell lines, including breast, ovarian, and prostate cancer.

SACM1L has also been shown to be a potential biomarker for various diseases, including cancer. The PI3K/Akt signaling pathway is involved in the regulation of various cellular processes, including cell growth, differentiation, and survival. The inhibition of SACM1L by small interfering RNA (siRNA) has been shown to reduce the growth and survival of cancer cells. This suggests that SACM1L may be a useful biomarker for the diagnosis and treatment of cancer.

Drugs that Target SACM1L

SACM1L is a drug target that has potential for the treatment of various diseases, including cancer. Drugs that target SACM1L have been shown to inhibit its catalytic activity and reduce the growth and survival of cancer cells.

One of the most promising drugs that targets SACM1L is a small interfering RNA (siRNA). SiRNA is a natural compound that can interact with RNA and prevent the translation of RNA into proteins. SiRNA has been shown to be a powerful tool for the inhibition of gene expression in various organisms, including cancer.

SACM1L is a good candidate forsiRNA therapy because of its unique structure and its involvement in cellular signaling. SiRNA can be designed to specifically target SACM1L and inhibit its catalytic activity. This can lead to the inhibition of downstream signaling pathways and the regression of cancer cells.

Another drug that targets SACM1L is a chemical compound called ML-862, which is a phosphatidylinositol inhibitor. ML-862 has been shown to inhibit the catalytic activity of SACM1L and has been shown to reduce the growth and survival of cancer cells.

Conclusion

SACM1L is an enzyme that plays a crucial role in

Protein Name: SAC1 Like Phosphatidylinositide Phosphatase

Functions: Phosphoinositide phosphatase which catalyzes the hydrolysis of phosphatidylinositol 4-phosphate (PtdIns(4)P) (PubMed:24209621, PubMed:27044890, PubMed:29461204, PubMed:30659099). Can also catalyze the hydrolysis of phosphatidylinositol 3-phosphate (PtdIns(3)P) and has low activity towards phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2) (By similarity). Shows a very robust PtdIns(4)P phosphatase activity when it binds PtdIns(4)P in a 'cis' configuration in the cellular environment, with much less activity seen when it binds PtdIns(4)P in 'trans' configuration (PubMed:29461204, PubMed:24209621, PubMed:30659099). PtdIns(4)P phosphatase activity (when it binds PtdIns(4)P in 'trans' configuration) is enhanced in the presence of PLEKHA3 (PubMed:30659099)

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•   protein structure and compound binding;
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•   expression level;
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