Protein Phosphatase 1A (PPM1A) is a member of the PP2C family of Ser/Thr protein phosphatases which are known to be negative regulators of cell stress response pathways. PPM1A has a broad specificity. PPM1A negatively regulates the activities of MAP kinases and MAP kinase kinases. Also, it negatively regulates TGF-beta signaling through dephosphorylating SMAD2 and SMAD3, resulting in their dissociation from SMAD4, nuclear export of the SMADs and termination of the TGF-beta-mediated signaling. In addition, PPM1A can dephosphorylate cyclin-dependent kinases, and thus may be involved in cell cycle control.
Protein phosphatase 1G; also known as Protein phosphatase 1C; Protein phosphatase 2C isoform gamma; Protein phosphatase magnesium-dependent 1 gamma; PP2C-gamma; PPM1G and PPM1C; is a cytoplasm protein which belongs to thePP2C family. PPM1G / PP2C-gamma is widely expressed. It is most abundant in testis; skeletal muscle; and heart. Alternatively spliced transcript variants encoding the same protein have been described. PP2C family members are known to be negative regulators of cell stress response pathways. PPM1G / PP2C-gamma is found to be responsible for the dephosphorylation of Pre-mRNA splicing factors; which is important for the formation of functional spliceosome. PPM1G / PP2C-gamma also plays a role in regulating cell cycle progression.
Protein Phosphatase 1G (PP1MG) is a cytoplasmic protein that belongs to the PP2C family. PPM1G is widely expressed; it is abundant in testis; skeletal muscle; and heart. PPM1G is a negative regulator of cell stress response pathways. PPM1G is responsible for the dephosphorylation of Pre-mRNA splicing factors; an important factor for the formation of functional spliceosome. PPM1G also plays a role in regulating cell cycle progression.
Serine/Threonine-Protein Phosphatase PP1-Υ Catalytic Subunit (PPP1CC) is a member of the PPP phosphatase family. It is essential for cell division, participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. PPP1CC colocalizes with SPZ1 in the nucleus, with URI1 at mitochondrion, Rapidly exchanges between the nucleolar, nucleoplasmic and cytoplasmic compartments. As a cofactor, PPP1CC binds one iron ion and one manganese ion per subunit.. In addition, PPP1CC may play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca2+/calmodulin dependent protein kinase II.
Protein Phosphatase 1 Regulatory Subunit 14A (PPP1R14A) belongs to the PP1 inhibitor family. PPP1R14A is mapped to chromosome 19q13.13-q13.2. PPP1R14A binds directly to protein kinase C and casein kinase I. Meantime; PPP1R14A is a phosphorylation-dependent inhibitor of smooth muscle myosin phosphatase. PPP1R14A is the inhibitor of PPP1CA. When phosphorylated; PPP1R14A has over 1000-fold higher inhibitory activity; creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction. In addition; inhibition of PPP1R14A also enhances contraction of smooth muscle in the absence of increment of intracellular Ca2+ concentration.
Protein Phosphatase 1 Regulatory Subunit 1A (PPP1R1A) is an inhibitor of protein-phosphatase 1. PPP1R1A is a cellular regulator of eIF2 alpha phosphorylation. In hormonal control of glycogen metabolism, IPP-1 protein plays important function. Hormones can elevate intracellular cAMP level and elevate IPP-1 activity. PPP1R1A activation caused cAMP increase , cAMP control over proteins that are not directly phosphorylated by PKA following a rise in intracellular calcium. IPP-1 is inactivated by calcineurin (PP2B). Multiple domains in IPP-1 target cellular PP1 complexes.
Inserisci la tua e-mail e seleziona le aree di interesse per ricevere le ultime novità, approfondimenti e promozioni.
Seleziona uno o più ambiti di interesse per ricevere comunicazioni più utili e mirate.
2025 TEMA Ricerca - All Rights Reserved.
