Junction-mediating and regulatory protein, p53 cofactor (JMY)

Junction-mediating and regulatory protein, p53 cofactor (JMY) is a multifunctional protein that acts both as a nuclear p53 cofactor and a cytoplasmic actin nucleation–promoting factor[1][2][3][4][5]. In the nucleus, JMY interacts with the coactivator p300 and enhances p53-dependent transcription and apoptosis, especially in response to DNA damage; this involves its translocation to the nucleus following stress[1][3][4]. Cytoplasmically, JMY contains tandem WH2 domains and a WWWCA region, allowing it to nucleate actin directly (in a Spire-like fashion) and/or activate the Arp2/3 complex, thus promoting cell migration and cytoskeletal remodeling[1][2][3][4]. JMY influences multiple cellular processes including cell motility, oocyte maturation, inflammatory cell migration, asymmetric division, and negative regulation of neurite outgrowth during neuronal differentiation[1][2][3][4]. JMY’s dysfunction or altered expression may impact cancer progression (via p53 pathway and migration), neurodevelopment, and has been linked to diseases such as spinocerebellar ataxia and glaucoma[5]. JMY is not currently considered a direct therapeutic target (such as a receptor, enzyme, or transporter), and no drugs are known to modulate its function directly[5].

Other names

Junction-mediating and regulatory proteinJMYFLJ37870WHAMM2WHDC1L3WAS protein homology region 2 domain containing 1-like 3junction-mediating and -regulatory proteinp53 cofactor