GENE INFLUENCES NFAT PHOSPHORYLATION

Gene influences NFAT Phosphorylation

Gene influences NFAT Phosphorylation

Introduction

The NH 2-terminal NFAT homology domain encodes several different sequences, including why PXIX, the region rich in Ser (RRS), and Ser-Pro (boxes SP)-rich NFAT regulation (18, 47). These sequences are found in all NFAT members. The reason is known for PXIX phosphatase calcineurin (3, 15), which dephosphorylates NFAT during activation. The kidnapping of the phosphatase calcineurin by the overexpression blocks the activation of NFAT PXIX pattern. The SRR and SP boxes are the main objectives of the phosphorylation of NFAT (4-6, 12-14, 44, 46, 58). Dephosphorylation of Ser residues in the SRR and SP boxes promotes nuclear localization of NFAT. Therefore, the dephosphorylation of NFAT homology domain, which is mediated by calcineurin, plays an important role in the activation of NFAT.

Gene influences the phosphorylation of NFAT

Once NFAT is dephosphorylated and transported to the nucleus, activated NFAT interacts with other transcription factors to induce gene expression. The interaction of NFAT with Fos-Jun (AP-1 complex), GATA, NFAT and MEF2 suggests that often works with elements made of DNA (7, 41, 43, 54, 56). Formation of a ternary complex induces the expression of NFAT targets, such as interleukin-2 (IL-2), IL-4, IL-5 and tumor necrosis factor alpha. However, the physiological function of NFAT in nonimmune tissues to be determined.

Multiple protein kinases, including MAPK protein (MAP) kinase group (ERK, JNK and p38 kinase), glycogen synthase kinase 3ß (GSK3ß), protein kinase A (PKA) and casein kinase 1a (CK1a) were shown to NFAT phosphorylation (4, 6, 12-14, 29, 46, 58). NFAT is phosphorylated on multiple Ser residues located in the conserved SRR and SP boxes. Phosphorylation of these residues Ser opposes the nuclear localization of NFAT either by promoting nuclear export or preventing nuclear import. For example, phosphorylation of Ser269 in NFATc1 (6) and NFATc4 Ser289 (12) can be ...