JMY (junction mediating and regulatory protein) is a transcription co-factor, originally identified as a p300-binding protein involved in p53-dependent transcription. Upon DNA damage, JMY is released from Mdm2 inhibition and forms a complex with Strap and p300. This complex recruits PRMT5 to activate the p53 response. Through regulation of p53-dependent transcription, JMY has important roles in the DNA damage response. In addition, JMY contains three carboxyl-terminal WH2 actin binding domains which are are commonly found in WASP family proteins. JMY can bind to actin and to the Arp2/3 complex, as well as direct the assembly of actin filaments in vitro. These actin-regulating effects of JMY may have important roles in cell migration. When slow migrating HL-60 cells are differentiated into highly motile neutrophil-like cells, JMY moves from the nucleus to the cytoplasm and is concentrated at the actin-rich leading edge of cells. The loss of JMY leads to decreased cell migration in HL-60 cells. Thus, JMY represents a new class of multifunctional actin assembly factors whose activity may be regulated by cellular localization.
Zuchero, J.B. et al. (2009) Nat Cell Biol. 11(4):451.
Shikama, N. et al. (1999) Molecular Cell 4:365.
*For more information, see UniProt Accession Q9QXM1
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
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