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Phosphorylation regulation

Figure 8. For any set of conditions, the greatest velocity that a muscle can shorten is attained when the total force opposing shortening is zero. Empirically, the maximum velocity of shortening increases with the degree of phosphorylation of myosin. This is seen as the straight line in the velocity-phosphorylation plane. The maximum force that a smooth muscle can develop is not increased by phosphorylation beyond about 25% phosphorylation. It seems therefore that past a point, phosphorylation regulates the rate at which work is being done rather than the force that can be developed. The force a muscle can develop if 25% myosin is phosphorylated is maximal and saturated however, the rate of doing work is not saturated and continues to increase with further phosphorylation. Figure 8. For any set of conditions, the greatest velocity that a muscle can shorten is attained when the total force opposing shortening is zero. Empirically, the maximum velocity of shortening increases with the degree of phosphorylation of myosin. This is seen as the straight line in the velocity-phosphorylation plane. The maximum force that a smooth muscle can develop is not increased by phosphorylation beyond about 25% phosphorylation. It seems therefore that past a point, phosphorylation regulates the rate at which work is being done rather than the force that can be developed. The force a muscle can develop if 25% myosin is phosphorylated is maximal and saturated however, the rate of doing work is not saturated and continues to increase with further phosphorylation.
In most tissues, where the primary role of the citric acid cycle is in energy-yielding metabohsm, respiratory control via the respiratory chain and oxidative phosphorylation regulates citric acid cycle activity (Chapter 14). Thus, activity is immediately dependent on the supply of NAD, which in turn, because of the tight couphng between oxidation and phosphorylation, is dependent on the availabihty of ADP and hence, ulti-... [Pg.134]

This class of receptors transmits signals carried by hormones and growth factors. The structure consists of an extracellular domain for binding ligands and a cytoplasmic enzyme domain. The function of kinases is to enable phosphorylation. Phosphorylation regulates most aspects of cell life. [Pg.44]

Modulation of ubiquitin ligases by phosphorylation Regulation of ubiquitin ligase activity by phosphorylation has been shown in the studies on a multisubunit ligase, APC. As the name implies, this complex is critical for cell cycle progression into anaphase. A recent study shows that a form of APC is also expressed in postmitotic neurons. [Pg.708]

Fujita-Becker, S., Durrwang, U., Erent, M., Clark, R. J., Geeves, M. A., and Manstein, D. J. (2005). Changes in Mg2+-ion concentration and heavy chain phosphorylation regulate the motor activity of a class-I myosin. / Biol. Chem. 280, 6064-6071. [Pg.190]

The activation of NHE-1 is associated with a phosphorylation of the exchanger protein on serine residues that are located in the C terminal cytoplasmic region of the protein (Saidet et al., 1990). The serine residue whose phosphorylation regulates Na+/H+ exchange and the kinase involved have not yet been identified. Phosphorylation of NHE-1 results in an increase in affinity of the exchanger protein for internal H+. As a consequence the dose-response curve for the activation of Na+ uptake by pHi shows a shift to higher pHi values. [Pg.158]

CF is caused by a defect in the CFTR protein. This protein is a cAMP- and phosphorylation-regulated chloride ion channel, important in maintaining osmotic gradients and the movement of water across epithelial membranes. [Pg.85]

Phosphorylation. Phosphorylation is a posttranslational modification that is reflected in close to 30% of eukaryotic gene products and almost 2% of the human genome-encoded protein kinases. Protein phosphorylation plays an essential role in intercellular communication during development, in physiological responses and homeostasis, and in the functioning of the nervous and immune systems. Reversible phosphorylation regulates many diverse... [Pg.866]

Piotrowicz, R.S., Hickey, E., and Levin, E.G., Heat shock protein 27 kDa expression and phosphorylation regulates endothelial cell migration, FASEB J., 12, 1481, 1998. [Pg.160]

Xavier C-P, Rosentreter A, Hofmann A et al. Phosphorylation regulates the quaternary structure and activity of coronin 3. Manuscript in preparation 2007. [Pg.70]

Leucettines, a family of marine sponge-derived2-aminoimidazolone alkaloids, are potent inhibitors of DYRKs (dual-specificity, tyrosine phosphorylation-regulated kinases) and CLKs (cdc2-like kinases), with potential therapeutic effect in AD [516],... [Pg.449]

Sellers JR, Spudich JA, Sheetz MP (1985) Light chain phosphorylation regulates the movement of smooth muscle myosin on actin filaments. J Cell Biol 101 1897-1902 Seto M, Sasaki Y, Sasaki Y (1990) Alteration in the myosin phosphorylation pattern of smooth muscle by phorbol ester. Am J Physiol 259 C769-C774 Sherry JMF, Gorecka A, Aksoy MO, Dabrowska R, Hartshorne DJ (1978) Roles of calcium and phosphorylation in the regulation of the activity of gizzard myosin. Biochemistry 17 4411-4418... [Pg.139]

Chen L F, Williams S A, Mu, Y, et al. (2005). NF-kappaB RelA phosphorylation regulates RelA acetylation. Mol. Cell. Biol. 25 7966-7975. [Pg.439]

EXAMPLE 10.18 How is the extent of uncoupling of oxidative phosphorylation regulated in brown adipose tissue (BAT) ... [Pg.319]


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See also in sourсe #XX -- [ Pg.234 ]

See also in sourсe #XX -- [ Pg.9 ]




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Extracellular regulated kinases phosphorylation

H3 phosphorylation and transcriptional regulation

NMDA receptors phosphorylation, regulation

Oxidative phosphorylation enzyme regulation

Oxidative phosphorylation regulation

Phosphorylation adenyl cyclase regulation

Phosphorylation enzyme regulation

Phosphorylation events, regulation

Phosphorylation intracellular calcium regulation

Phosphorylation metabolic regulation

Phosphorylation thick filament regulation

Phosphorylation thin filament regulation

Phosphorylation, protein regulation

Protein Phosphorylation and Regulation of Glycogen Metabolism

Protein tyrosine phosphorylation intracellular calcium regulation

Receptor tyrosine kinases phosphorylation, regulation

Regulation of Enzyme Activity by Phosphorylation

Regulation of Glycogen Phosphorylase by Phosphorylation

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