High impact information on Ppm1a

• Accordingly, IpgD and PtdIns5P production specifically activates a class IA PI 3-kinase via a mechanism involving tyrosine phosphorylations [1].
• Sequential activation of class IB and class IA PI3K is important for the primed respiratory burst of human but not murine neutrophils [2].
• In addition, inhibition by IC87114 of the major class IA PI3K catalytic subunit expressed in lymphocytes, p110delta, blocked transition of DN to DP cells in embryonic day 14.5 fetal thymic organ culture without affecting cell viability [3].
• In the absence of phosphatase and tensin homolog deleted on chromosome 10, where class IA PI3K signals would be amplified, the DN to DP transition was accelerated [3].
• The p85{alpha} Regulatory Subunit of Class IA Phosphoinositide 3-Kinase Regulates beta-Selection in Thymocyte Development [3].

Biological context of Ppm1a

• Class IA phosphatidylinositide 3-kinases, rather than p110 gamma, regulate formyl-methionyl-leucyl-phenylalanine-stimulated chemotaxis and superoxide production in differentiated neutrophil-like PLB-985 cells [4].
• Thus, the level of involvement of IA in controlling programmed cell death of hypothalamic cells depends on the age of the animals [5].

Associations of Ppm1a with chemical compounds

• Phosphorylation of PP2C alpha was enhanced two-fold by the addition of okadaic acid to the culture medium, but addition of cyclosporin A had no such effect [6].
• The aim of this study was to identify the involvement of interferon-alpha (IA) in controlling apoptosis of cells of the hypothalamo-hypophyseal-adrenocortical system (HHACS) in young and aged mice in conditions of hyperoxia [5].

Enzymatic interactions of Ppm1a

• These results suggest that the expressed PP2C alpha is phosphorylated by a casein kinase II-like protein kinase and dephosphorylated by PP1 and/or PP2A in COS7 cells [6].

References