Background[1-3]
Phosphorylated beta-arrestin 1 antibody is a type of polyclonal immunoglobulin that can specifically bind to phosphorylated beta-arrestin 1. It is mainly used in immunological experiments to detect phosphorylated beta-arrestin 1.
β-arrestins are a group of multifunctional small molecule proteins that play a very important role in regulating intracellular signal transduction. Its classic role is to participate in the desensitization and endocytosis of G protein-coupled slippery receptors. Recent studies have found that β-arrestins, especially β-arrestin-1 protein, serve as “traffic workers” for signal transduction and are also involved in signal transduction activated by many non-G protein-coupled receptors. They are involved in proteasomal degradation and cell apoptosis. and plays an important role in various cell signal transductions.
G Protein-Coupled Receptors (GPCRs) are the collective name for a large class of membrane protein receptors. What this type of receptors have in common is that they all have seven transmembrane α-helices in their three-dimensional structure, and the C-terminus of their peptide chain is connected to the intracellular structure of the fifth and sixth transmembrane helices (counted from the N-terminus of the peptide chain). Both rings (the third intracellular ring) have binding sites for G proteins (guanylate-binding proteins). So far, research shows that G protein-coupled receptors are only found in eukaryotes and are involved in many cell signal transduction processes. In these processes, G protein-coupled receptors can bind chemicals in the environment around cells and activate a series of signaling pathways within the cells, ultimately causing changes in cell status.
Apply[4][5]
For functional study of β-arrestin 1 and protein kinase B (PKB/Akt) in the ecdysing hormone signaling pathway of Helicoverpa armigera
Using the lepidopteran insect Helicoverpa armigera as research material, exploring the function and mechanism of P-arrestin 1 in the desensitization of ecdysone signals is of great significance to enrich the regulatory mechanism of animal sterol hormones. Insulin is an important hormone in regulating insect development. Exploring the role of Akt in ecdysone signaling antagonizing insulin signaling will provide new evidence for further understanding the molecular mechanism of bollworm development and the mechanism by which insulin and ecdysone coordinately regulate insect development.
Experimental results and conclusions: 1. β-arrestinl is involved in the termination of ecdysone signaling. Western blot experiments found that β-arrestinl is highly expressed in the epidermis, midgut, and fat body during metamorphosis. Interfering with β-arrestinl in larvae can lead to premature Pupation and the formation of chimeric pupae, and interference and cell line overexpression experiments have shown that β-arrestinl can reduce the expression of 20E response genes. Korea lg
Further immune cell experiments found that 20E induced β-arrestinl to migrate from the cytoplasm to the cell membrane and interact with ErGPC R1. GPCR inhibitors and PKC inhibitors could inhibit the 20E-induced phosphorylation of β-arrestinl and its transfer to the cell membrane. migration. Further mutation experiments found that 20E regulates the phosphorylation and translocation of β-arrestinl at serine 170 and 234 amino acids.
These results indicate that 20E induces β-arrestin1 phosphorylation through ErGPCR1- and PKC-signaling; phosphorylated β-arrestin1 migrates from the cytoplasm to the cell membrane and interacts with ErGPCRl to block 20E signaling in a feedback regulatory manner. This article elucidates the mechanism of 20E signal termination and enriches the non-genomic signal transduction pathways of animal steroid hormones.
2. Ecdysone antagonizes insulin signaling by inhibiting Akt phosphorylation. Interfering with Akt from armigera cell lines or high concentrations of 20E can upregulate the expression of apoptosis-related genes, leading to cell apoptosis.
