Mammalian sprouty proteins assemble into large monodisperse particles having the properties of intracellular nanobatteries

Xinle Wu, Peter B. Alexander, Ying He, Masahide Kikkawa, Pia D. Vogel, Steven L. McKnight

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Sprouty proteins act as intracellular inhibitors of receptor tyrosine kinase signaling. Here we show that the mammalian Sprouty2 protein contains an iron-sulfur complex that can exist in an oxidized, reduced, or nitrosylated state. Purified Sprouty2 assembles into large monodisperse spheres containing ≈24 polypeptides per particle. Biochemical experiments indicate that the charge state of the iron within Sprouty2 particles may be insulated from ambient intracellular redox. These features offer the possibility that Sprouty2 particles are capable of receiving, maintaining, and dissipating electrical charge in a manner formally equivalent to a battery.

Original languageEnglish (US)
Pages (from-to)14058-14062
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume102
Issue number39
DOIs
StatePublished - Sep 27 2005

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Iron-Sulfur Proteins
Receptor Protein-Tyrosine Kinases
Oxidation-Reduction
Iron
Peptides
Proteins

Keywords

  • Iron-sulfur
  • Multisubunit
  • Redox

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

Mammalian sprouty proteins assemble into large monodisperse particles having the properties of intracellular nanobatteries. / Wu, Xinle; Alexander, Peter B.; He, Ying; Kikkawa, Masahide; Vogel, Pia D.; McKnight, Steven L.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 102, No. 39, 27.09.2005, p. 14058-14062.

Research output: Contribution to journalArticle

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