Mapping of glycolytic enzyme-binding sites on human erythrocyte band 3

Haiyan Chu, Philip S. Low

Research output: Contribution to journalArticle

99 Scopus citations

Abstract

Previous work has shown that GAPDH (glyceraldehyde-3-phosphate dehydrogenase), aldolase, PFK (phosphofructokinase), PK (pyruvate kinase) and LDH (lactate dehydrogenase) assemble into a GE (glycolytic enzyme) complex on the inner surface of the human erythrocyte membrane. In an effort to define the molecular architecture of this complex, we have undertaken to localize the binding sites of these enzymes more accurately. We report that: (i) a major aldolase-binding site on the erythrocyte membrane is located within N-terminal residues 1-23 of band 3 and that both consensus sequences D6DYED 10 and E19EYED23 are necessary to form a single enzyme-binding site; (ii) GAPDH has two tandem binding sites on band 3, located in residues 1-11 and residues 12-23 respectively; (iii) a PFK-binding site resides between residues 12 and 23 of band 3; (iv) no GEs bind to the third consensus sequence (residues D902EYDE906) at the C-terminus of band 3; and (v) the LDH- and PK-binding sites on the erythrocyte membrane do not reside on band 3. Taken together, these results argue that band 3 provides a nucleation site for the GE complex on the human erythrocyte membrane and that other components near band 3 must also participate in organizing the enzyme complex.

Original languageEnglish (US)
Pages (from-to)143-151
Number of pages9
JournalBiochemical Journal
Volume400
Issue number1
DOIs
StatePublished - Nov 15 2006

Keywords

  • Band 3-peripheral protein interaction
  • Cytoplasmic domain of band 3
  • Erythrocyte cytoskeleton
  • Erythrocyte membrane structure
  • Glycolysis
  • Glycolytic enzyme complex

ASJC Scopus subject areas

  • Biochemistry

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