Disease relevance of Ppp1r12a

• The MBSP may mediate rapid nongenomic steroid effects that contribute to steroid-induced cataracts [1].

High impact information on Ppp1r12a

• Activation of myosin phosphatase targeting subunit by mitosis-specific phosphorylation [2].
• Antibody probing of this complex detected hsc70, hsp90, two isoforms of the catalytic subunit of PP1, PP1C alpha and PP1C delta, as well as the M regulatory subunit of PP1 (PP1M) [3].
• Isoforms of the smooth muscle myosin phosphatase targeting subunit 1 (MYPT1) are generated by cassette-type alternative splicing of exons [4].
• Splicing of a myosin phosphatase targeting subunit 1 alternative exon is regulated by intronic cis-elements and a novel bipartite exonic enhancer/silencer element [4].
• Three monoclonal antibodies (M110, A82, and A917) were obtained by fusing myeloma cells and spleen cells from mice immunized with partially purified rabbit mammary gland prolactin (PRL) receptors [5].

Biological context of Ppp1r12a

• Phosphorylation of Thr695 and Thr850 on the myosin phosphatase target subunit: inhibitory effects and occurrence in A7r5 cells [6].
• Myosin phosphatase targeting subunit 1 (MYPT1) isoforms are generated by cassette-type alternative splicing of exons in the central and 3' portion of the transcript [7].
• The N-terminus of the M110 subunit from rat aorta contains seven ankyrin repeats, while the C-terminus of the M21 subunit from chicken gizzard contains a leucine zipper motif [8].
• MP is composed of 3 subunits: a catalytic subunit of type 1 phosphatase, PPlc; a targeting subunit, termed myosin phosphatase target subunit, MYPT; and a smaller subunit, M20, of unknown function [9].

Anatomical context of Ppp1r12a

• A myosin phosphatase targeting subunit isoform transition defines a smooth muscle developmental phenotypic switch [10].
• PP1M activity was high in synaptosomes isolated from the cerebral cortex, but was relatively low in the postsynaptic densities [11].
• M110 anti PRL-R was internalised in endosomes and detected mainly in microvesicular bodies during a one hour incubation [12].
• One major (Mb I) and two minor (Mbs II and III) myoglobins, were isolated by a heat-denaturation-gel-filtration-chromato-focusing procedure from aqueous extract of rat skeletal muscles [13].

Associations of Ppp1r12a with chemical compounds

• The phosphorylation level of myosin phosphatase target subunit 1 (MYPT1) at the inhibitory site was also significantly higher in SHRSP, and the phosphorylation levels in both VSMCs were strongly inhibited to a similar extent by treatment with Y-27632, a Rho-kinase inhibitor [14].
• However, its C-terminal half (downstream from the M58 fragment) is required for inhibition by arachidonic acid [15].

Other interactions of Ppp1r12a

• Major sites for Rho-kinase on the myosin phosphatase target subunit (MYPT1) are Thr695 and Thr850 [6].

Analytical, diagnostic and therapeutic context of Ppp1r12a

• Analysis of lysates of brain regions for MYPT1 and PP1M by Western blots using anti-MYPT1 antibodies and by phosphatase assays with myosin as substrate suggested a ubiquitous distribution [11].

References