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.
PPP3CA, also known as protein phosphatase 2B, is a member of the PPP phosphatase family, PP-2B subfamily. It is the alpha catalytic subunit of protein phosphatase 2B (PP2B). PP2B is a holoenzyme that is comprised of a catalytic subunit associated with regulatory subunits. It is a calcium regulated enzyme that is activated by calmodulin and participates in the signaling cascades involved in development of the nervous, cardiovascular, and musculoskeletal systems. PPP3CA activates the T cells of the immune system and can be blocked by drugs. It also activates NFATc (a transcription factor) by dephosphorylating it. The activated NFATc is subsequently translocated into the nucleus, where it upregulates the expression of interleukin 2. PPP3CA interacts with CRTC2, MYOZ1, MYOZ2 and MYOZ3. It also interacts with DNM1L. The interaction dephosphorylates DNM1L and regulates its translocation to mitochondria.
PPP3R1 belongs to the calcineurin regulatory subunit family. It is a regulatory subunit of calcineurin. Calcineurin is composed of two subunits: calcineurin A (CnA) and calcineurin B (CnB). Dephosphorylation of the nuclear factor of activated T-cells (NF-AT) by Calcineurin is essential for NF-AT activation; nuclear translocation; and early gene expression in T-cells. PPP3R1 is a Ser/Thr-specific calcium and calmodulin-dependent protein phosphatase which takes a vital part in the T cell activation pathway. PPP3R1 is involved in protein dephosphorylation; NFAT protein import into nucleus (ortholog) and epithelial to mesenchymal transition (ortholog). It participates in calcineurin signaling pathway; mitogen activated protein kinase signaling pathway. PPP3R1 interacts with (+)-pilocarpine; 2;4-dinitrotoluene and ammonium chloride. It contains four EF-hand domains and four functional calcium-binding sites. PPP3R1 play an improtant role in the T cell activation pathway.
Palmitoyl-protein thioesterase 1(PPT-1 for short), also known as Palmitoyl-protein hydrolase 1, belongs to the palmitoyl-protein thioesterase family. It is a small glycoprotein involved in the catabolism of lipid-modified proteins during lysosomal degradation. This enzyme removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. Defects in PPT1 are the cause of neuronal ceroid lipofuscinosis type 1.
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