Unusual partitioning behavior of CaATPase in dipalmitoylphosphatidylethanolamine/dielaidoylphosphatidylcholine++ + mixtures

Jaworsky, Mark; Mendelsohn, Richard

doi:10.1016/s0006-3495(87)83211-3

Cited by 8 publications

(1 citation statement)

References 31 publications

(44 reference statements)

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“…Similarly, inclusion of diacylglycerol in the monolayer also raises the maximum surface pressure into which calcineurin will insert (Table ). Although the percentage of phosphatidylserine at which membrane binding is within the physiologic range exceeds the measured percentage of phosphatidylserine found in biomembranes (10−20%) ( , ), the existence of locally high concentrations, or “patches”, of phospholipids and/or diglyceride has been postulated in numerous studies ( − ). A stimulus-specific mechanism of achieving locally high concentrations of phospholipid/diglyceride might serve as a mechanism for regulating calcineurin localization in vivo.…”

Section: Discussionmentioning

confidence: 99%

Determinants of Calcineurin Binding to Model Membranes

1997

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The biochemical factors that lead to membrane targeting of the Ser/Thr protein phosphatase calcineurin were examined using model phospholipid membranes. The interaction of myristoyl- and non-myristoylcalcineurin with lipid surfaces was investigated as a function of negatively charged phospholipids, diacylglycerol, Ca2+, and calmodulin. The data indicate that calcineurin binding to phospholipid monolayers both is myristoyl-independent and is mediated by anionic phospholipids and/or diacylglycerol. Although the effect of Ca2+ on calcineurin-lipid binding is minor, calmodulin altered the binding of calcineurin to the lipid membrane in a Ca2+-dependent manner. Experiments with a constitutively active form of calcineurin that does not bind calmodulin indicated that the effect required the interaction of calcineurin with calmodulin. Our results suggest that phosphatidylserine, diaclyglycerol, and calmodulin may mediate the lipid binding properties of calcineurin in vivo.

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Section: Discussionmentioning

confidence: 99%

Determinants of Calcineurin Binding to Model Membranes

1997

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Differential scanning calorimetry study of glycogen phosphorylaseb-detergent interactions

Centeno

Fernandez-Salguero

Laynez

et al. 1992

J Bioenerg Biomembr

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The overall thermal denaturation of glycogen phosphorylase b is irreversible and our results conform to the theoretical prediction of a reversible process followed by a slower irreversible process. The basic thermodynamic parameters of glycogen phosphorylase b denaturation have been worked out and found to be: critical temperature 57.0 +/- 0.5 degrees C, transition half-width 8 +/- 1 degrees C, and calorimetric enthalpy change and Van't Hoff enthalpy change of the denaturation process 450 +/- 50 and 105 +/- 15 kcal/mol of enzyme monomer, respectively, at pH 7.4. These parameters have been found to be largely altered by the detergents octylglucoside, cholate, and deoxycholate at or below their critical micelle concentration, but not by Triton X-100 nor by lecithin liposomes. Organic solvents, such as dimethyl sulfoxide and methanol, and the presence of sarcoplasmic reticulum membranes produces an alteration of the denaturation thermogram of glycogen phosphorylase b similar to that produced by the above-mentioned detergents. These results allow us to hypothesize that hydrophobic domains of glycogen phosphorylase b are involved in its association to sarcoplasmic reticulum membranes in the sarcoplasmic reticulum/glycogenolytic complex of mammalian skeletal muscle.

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