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Myosin phosphatase target subunit 1, which is also called the myosin-binding subunit of myosin phosphatase, is one of the subunits of myosin phosphatase. Additionally we are shipping PPP1R12A Kits (6) and PPP1R12A Proteins (4) and many more products for this protein.
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Human Monoclonal PPP1R12A Primary Antibody for WB - ABIN968767
Chen, Chen, Alessi, Campbell, Shanahan, Cohen, Cohen: Molecular cloning of cDNA encoding the 110 kDa and 21 kDa regulatory subunits of smooth muscle protein phosphatase 1M. in FEBS letters 1995
Show all 3 references for ABIN968767
revealed the presence of two MYPT1 isoforms, full length and variant 2 in human intestinal (Caco-2) epithelial cells and isolated intestinal epithelial cells from mice
phosphorylation of MYPT1 T694, but not T852, mediates force maintenance in bladder smooth muscle.
Constitutive phosphorylation of myosin phosphatase targeting subunit-1 in smooth muscle
Maturation of mesenteric artery smooth muscle involves TRA2beta (show TRA2B Antibodies) mediated Mypt1 exon 24 splicing.
The role of MYPT1 in vascular smooth muscle was investigated in adult MYPT1 smooth muscle specific knock-out mice. MYPT1 deletion enhanced phosphorylation of myosin regulatory light chain and contractile force in isolated mesenteric arteries.
MYPT1 is not essential for smooth muscle function in mice but regulates the Ca(2 (show CA2 Antibodies)+) sensitivity of force development and contributes to intestinal phasic contractile phenotype.
Tra2beta (show TRA2B Antibodies), by regulating the splicing of Mypt1 E23, sets the sensitivity of smooth muscle to cGMP-mediated relaxation.
Organ-specific mechanisms involving MYPT1, M-RIP (show MPRIP Antibodies), and CPI-17 (show PPP1R14A Antibodies) are critical to regulating basal LC20 (show MYL9 Antibodies) phosphorylation in gastrointestinal smooth muscles.
Findings define a new conserved pathway in which sexual development and pregnancy mediate smooth and striated (show NSDHL Antibodies) muscle adaptations through SMTNL1 and MYPT1.
a reduction in the protein level of MYPT1 (LZ+) is involved in nitrate tolerance; this may result in part from a proteasome-dependent degradation of MYPT1 (LZ+)
Study revealed the presence of two MYPT1 isoforms, full length and variant 2 in human intestinal (Caco-2) epithelial cells and isolated intestinal epithelial cells from mice.
These results indicate that PPP1R12A indeed plays a role in skeletal muscle insulin (show INS Antibodies) signaling
the relative expression of LZ+/LZ (show LYZ Antibodies)- MYPT1 isoforms, in part, defines the vascular response to NO and NO based vasodilators, and therefore, plays a role in the regulation of vascular tone in both health and disease
Expression of NUAK1 (show NUAK1 Antibodies) is controlled by cyclin-dependent kinase (show CDK1 Antibodies), PLK1 (show PLK1 Antibodies), and the SCFbetaTrCP (Skp, Cullin and F-boxbetaTrCP) E3 ubiquitin ligase (show MUL1 Antibodies) complex.
distinct roles of two inhibitory phosphorylation sites of MYPT1
in apoptotic cells, the myosin-binding domain of myosin phosphatase targeting subunit 1 is cleaved by caspase-3, and the cleaved MYPT1 is strongly phosphorylated at Thr-696 and Thr-853, phosphorylation of which is known to inhibit myosin II binding
results suggested that during atherosclerosis progression oxidative stress mediates the downregulation of MYPT1, which may inhibit smooth muscle cell migration and contribute to the aberrant contractility
Calcineurin (show PPP3CA Antibodies) may modulate the phosphorylation level of MLC20 (show MYL12B Antibodies) by influencing the phosphorylation state of MYPT1 to regulate endothelial barrier function.
Mypt1 colocalizes outside the nucleus with Nkx2.5 in a manner dependent on Wnt signaling and Rho-associated protein kinase.
These findings provide evidence for the involvement of a particular PP1 (show PPA1 Antibodies) complex, PPP1R12A/PP1cdelta, in insulin (show INS Antibodies) signaling.
Myosin phosphatase target subunit 1, which is also called the myosin-binding subunit of myosin phosphatase, is one of the subunits of myosin phosphatase. Myosin phosphatase regulates the interaction of actin and myosin downstream of the guanosine triphosphatase Rho. The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate (GTP)-bound, active form of RhoA (GTP.RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase, which regulates the extent of phosphorylation of MLC. Rho-associated kinase (Rho-kinase), which is activated by GTP. RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase. Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased phosphorylation of MBS and MLC. Thus, Rho appears to inhibit myosin phosphatase through the action of Rho-kinase. Several transcript variants encoding different isoforms have been found for this gene.
myosin phosphatase target subunit 1
, myosin phosphatase, target subunit 1
, myosin phosphatase-targeting subunit 1
, protein phosphatase 1 regulatory subunit 12A
, myosin binding subunit
, protein phosphatase 1, regulatory (inhibitor) subunit 12A
, protein phosphatase myosin-binding subunit
, protein phosphatase subunit 1M
, serine/threonine protein phosphatase PP1 smooth muscle regulatory subunit M110
, smooth muscle myosin phosphatase myosin-binding subunit
, 130 kDa myosin-binding subunit of smooth muscle myosin phophatase
, 130 kDa myosin-binding subunit of smooth muscle myosin phosphatase
, 133kDa myosin-binding subunit of smooth muscle myosin phosphatase (M133)
, PP1M subunit M110