Open AccessMammalian sprouty proteins assemble into large monodisperse particles having the properties of intracellular nanobatteries
Author(s) -
Xiaohong Wu,
Peter Alexander,
Ying He,
Masahide Kikkawa,
Pia D. Vogel,
Steven L. McKnight
Publication year - 2005
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.0506714102
Subject(s) - intracellular , dispersity , biophysics , chemistry , redox , microbiology and biotechnology , biochemistry , biology , organic chemistry
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 approximately 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.