Control of erythrocyte metabolism by redox-regulated tyrosine phosphatases and kinases

Philip Low, A. Kiyatkin, Q. Li, M. L. Harrison

Research output: Contribution to journalArticle

11 Scopus citations

Abstract

We wish to elaborate a novel mechanism of metabolic regulation mediated by cytoplasmic tyrosine phosphatases and kinases. Briefly we propose that phosphofructokinase, aldolase, and glyceraldehyde-3-phosphate dehydrogenase (G3PDH) bind reversibly to the N-terminus of the cytoplasmic domain of band 3. Once the enzymes are bound, they are inhibited; however, upon release they are restored to full activity. We demonstrate that control of enzyme binding and consequently control of substrate flow down the pathway is executed by phosphorylation of Tyr 8 and Tyr 21 within the glycolytic enzyme binding site at the N-terminus of band 3. This phosphorylation results in obstruction of enzyme binding, leading to enzyme activation. Importantly, the tyrosine kinase that phosphorylates band 3 is activated by oxidation, while the tyrosine phosphatase that dephosphorylates band 3 is inhibited by the same redox changes. Consequently, treatment of red cells wih oxidants such as H2O2 and ferricyanide can enhance both tyrosine phosphorylation of the N-terminus of band 3 and glycolysis in a coordinate manner. Because oxidant entry into the cell is not essential, a plasma membrane electron transport pathway is believed to mediate the oxidant's effects.

Original languageEnglish (US)
Pages (from-to)196-202
Number of pages7
JournalProtoplasma
Volume184
Issue number1-4
DOIs
StatePublished - Mar 1 1995

Keywords

  • Glycolysis
  • Pentose phosphate pathway
  • Plasma membrane redox shuttle
  • Tyrosine kinase

ASJC Scopus subject areas

  • Cell Biology
  • Plant Science

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