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Mypt1 E24 splice variants tune arterial reactivity and could be worthy targets for lowering vascular resistance in disease states.
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.
Thus, Cyclin A (show CCNA2 Antibodies)/Cdk1 (show CDK1 Antibodies) phosphorylation primes MYPT1 for Plk1 (show PLK1 Antibodies) binding. These data demonstrate cross-regulation between Cyclin A (show CCNA2 Antibodies)/Cdk1 (show CDK1 Antibodies)-dependent and Plk1 (show PLK1 Antibodies)-dependent phosphorylation of substrates during mitosis to ensure efficient correction of kinetochore microtubule attachment errors necessary for high mitotic fidelity.
NO-induced cGMP signaling modulated RhoA/ROCK signaling in platelets, leading to the disinhibition of MLCP to control the phosphorylation of MLC and remodeling of platelet actin cytoskeleton.
The authors call the mutual sequestration mechanism through which pCPI-17 and myosin light-chain phosphatase interact inhibition by unfair competition: myosin light-chain phosphatase protects pCPI-17 from other phosphatases, while pCPI-17 blocks other substrates from the active site of myosin light-chain phosphatase.
Myosin light chain phosphatase (MLCP) is a master regulator of smooth muscle responsiveness to stimuli. (review)
BLT2 (show LTB4R2 Antibodies) ligation facilitates F-actin assembly with the upregulated phosphorylation of MYPT1.
Lipolysis-stimulated lipoprotein receptors (LSRs) localized to bicellular junctions in association with myosin regulatory light chain 2 (MRLC2 (show MYL12B Antibodies)) at low cell densities and to tricellular contacts when myosin phosphatase target subunit 1 (MYPT1) localized to the bicellular regions.
miR (show MLXIP Antibodies)-30d and/or its target gene MYPT1 may serve as novel prognostic markers of PCa (show FLVCR1 Antibodies). miR (show MLXIP Antibodies)-30d promotes tumor angiogenesis of PCa (show FLVCR1 Antibodies) through MYPT1/c-JUN (show JUN Antibodies)/VEGFA (show VEGFA Antibodies) pathway.
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
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