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- _4 value "Finally, an interaction site for the conserved NH2-terminal K-[GS]-IL- K motif of inhibitor-2 has been mapped near the entrance of the RVXF-binding channel (90). Some R subunits, such as the Neurabins and the Mypts (see sect. VII, A and B), interact with PP1 in an isoform-specific manner, indicating that PP1 also contains isoform-specific regulatory binding sites. The R subunits bring PP1 in close proximity to its substrates by anchoring the phosphatase in specific cellular compartments via targetting motifs or domains. Some R subunits block the activity of PP1 by acting as pseudosubstrates (see sects. VIIB and IXA) or by inducing conformational changes (see sect. IXB). The substratespecifying effect of some R subunits (G subunits, Mypts, AKAP149) implies both an increased activity toward some substrates and a decreased activity toward other substrates. The surface of PP1 is relatively open, and no peptide binding cleft is evident, in accordance with its broad substrate specificity (33). One can therefore envisage that the binding of R subunits to PP1 restricts the accessibility of the catalytic site, either by causing steric hindrance or by inducing conformational changes. At least in some instances, the substrate-specifying activity may stem from the fact that the R subunits are themselves substrates (see sects. IIIB and VIC) or have binding sites for specific substrates (see sect. VB). III. CELL DIVISION AND MEIOSIS Mutations of PP1 in various fungi and in the fruitfly, or microinjection of PP1-neutralizing antibodies or antisense PP1 oligonucleotides in cultured mammalian cells, all result in a mitotic arrest or a deficient cytokinesis (24, 31, 79, 114, 131, 172, 286, 329)." provenance.