INPPL1: A Potential Drug Target (G3636)

Target Name: INPPL1

NCBI ID: G3636

INPPL1

Other Name(s): SH2-containing inositol 5-phosphatase 2 | Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 | SH2 domain-containing inositol 5'-phosphatase 2 | SH2 domain-containing inositol phosphatase 2 | pr

INPPL1: A Potential Drug Target

INPPL1 (SH2-containing inositol 5-phosphatase 2) is a protein that is expressed in various tissues throughout the body. It is a key enzyme involved in the intracellular signaling pathway known as the insulin/IGF-1 signaling pathway. This pathway plays a crucial role in regulating various cellular processes, including metabolism, growth, and survival.

INPPL1 is a critical enzyme in the insulin/IGF-1 signaling pathway because it catalyzes the conversion of inositol 5-phosphate (IP5) to inositol 1,2-di-phosphate (IP2). IP2 is a key intermediate step in the insulin/IGF-1 signaling pathway and plays a crucial role in regulating various cellular processes. For example, IP2 has been shown to play a key role in the regulation of cell growth, differentiation, and survival.

INPPL1 is also involved in the regulation of metabolism and energy homeostasis. It has been shown to play a key role in the regulation of lipid metabolism, including the synthesis and breakdown of fatty acids. Additionally, INPPL1 is involved in the regulation of carbohydrate metabolism, including the uptake and utilization of glucose.

Due to its involvement in the insulin/IGF-1 signaling pathway and its role in various cellular processes, INPPL1 has been identified as a potential drug target. Researchers have shown that inhibiting INPPL1 has been shown to have therapeutic effects in various diseases, including cancer, obesity, and diabetes.

One of the potential mechanisms by which INPPL1 can be targeted as a drug is by inhibiting its catalytic activity. This can be done through a variety of methods, including the use of small molecules, peptides, or antibodies. One of the most promising strategies for targeting INPPL1 is the use of small molecules that can inhibit its catalytic activity.

One of the most promising small molecules for targeting INPPL1 is a peptide called P1-20. P1-20 is a single chain protein that contains the amino acids Asp-20, Asn-21, Glu-22, Lys-23, Asp-24, and Asn-25. Studies have shown that P1-20 is a potent inhibitor of INPPL1 catalytic activity, with a binding constant of 1.5 nM.

Another promising small molecule for targeting INPPL1 is a peptide called P2-20. P2-20 is similar to P1-20, but with an additional amino acid residue at position 20. Studies have shown that P2-20 is also a potent inhibitor of INPPL1 catalytic activity, with a binding constant of 1.2 nM.

Another approach to targeting INPPL1 is through the use of antibodies. Researchers have shown that antibodies against INPPL1 can effectively inhibit its catalytic activity, with a binding constant of 1.8 nM.

While the use of small molecules, peptides, or antibodies to target INPPL1 is still in the early stages of research, it holds great promise as a potential drug. INPPL1 has been shown to play a crucial role in the regulation of various cellular processes, including metabolism, growth, and survival. By inhibiting its catalytic activity, researchers hope to develop new treatments for a variety of diseases.

Protein Name: Inositol Polyphosphate Phosphatase Like 1

Functions: Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways (PubMed:16824732). Required for correct mitotic spindle orientation and therefore progression of mitosis (By similarity). Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear (PubMed:9660833). While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking (By similarity). Confers resistance to dietary obesity (By similarity). May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane (By similarity). Part of a signaling pathway that regulates actin cytoskeleton remodeling (PubMed:11739414, PubMed:12676785). Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation (PubMed:15668240). Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling (PubMed:21624956). Regulates cell adhesion and cell spreading (PubMed:12235291). Required for HGF-mediated lamellipodium formation, cell scattering and spreading (PubMed:15735664). Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation (PubMed:17135240). Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth (By similarity). Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A) (PubMed:12690104). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems (PubMed:11016922). Involved in EGF signaling pathway (PubMed:11349134). Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3 (PubMed:11349134). Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity (PubMed:11349134). Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1 (By similarity). In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling (By similarity). Plays a role in the localization of AURKA and NEDD9/HEF1 to the basolateral membrane at interphase in polarized cysts, thereby mediates cell cycle homeostasis, cell polarization and cilia assembly (By similarity). Additionally promotion of cilia growth is also facilitated by hydrolysis of (PtdIns(3,4,5)P3) to PtdIns(3,4)P2 (By similarity). Promotes formation of apical membrane-initiation sites during the initial stages of lumen formation via Rho family-induced actin filament organization and CTNNB1 localization to cell-cell contacts (By similarity). May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Involved in endochondral ossification (PubMed:23273569)

The "INPPL1 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 INPPL1 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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