Structural stability of the erythrocyte anion transporter, band 3, in different lipid environments. A differential scanning calorimetric study

L. R. Maneri, P. S. Low

Research output: Contribution to journalArticle

59 Scopus citations

Abstract

In order to understand how subtle variations in lipid structure can influence the stability of an integral membrane protein, the purified, delipidated anion transport domain of human erythrocyte band 3 was reconstituted into a series of well-defined lipids and examined by differential scanning calorimetry. From the calorimetric scans, plots of denaturation temperature (T(m)), enthalpy (ΔH(d)), and heat capacity (ΔC(p)(d)) as a function of phospholipid chain length, degree of unsaturation, headgroup type, and cholesterol content were constructed. The data show that the stability of the 55,000-dalton membrane-spanning domain of band 3 is exquisitely sensitive to the acyl chain length of its phospholipid environment, increasing almost linearly from a T(m) of 47°C in dimyristoleylphosphatidylcholine (C14:1) to 66°C in dinervonylphosphatidylcholine (C24:1). The integral domain was also found to be significantly stabilized by increasing the degree of saturation of the fatty acyl chains and by elevating the cholesterol content of the membrane. Although band 3 was native in all reconstituted lipid system, the transport protein's stability was clearly much greater in zwitterionic lipids (phosphatidylethanolamine and phosphatidylcholine) than anionic lipids (phosphatidylserine and phosphatidylglycerol). Enthalpy and Δ(p)(d) values were generally within the ranges expected of globular proteins in the various reconstituted systems, except the values for the anionic and polyunsaturated phospholipids were anomalously low. Much of the data can be accounted for by the hypothesis that band 3 has a long hydrophobic cross-section and that a close match between the hydrophobic zone of the membrane-spanning protein and the nonpolar region of the bilayer is necessary for maximum protein stability. Because the integral domain of band 3 may be structurally representative of a larger group of transport proteins, the data should be useful in interpreting structural observations on protein-lipid interactions in other membrane systems.

Original languageEnglish (US)
Pages (from-to)16170-16178
Number of pages9
JournalJournal of Biological Chemistry
Volume263
Issue number31
StatePublished - 1988

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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