A Phytochrome Sensory Domain Permits Receptor Activation by Red Light

Eva Reichhart, Alvaro Ingles-Prieto, Alexandra Madelaine Tichy, Catherine McKenzie, Harald Janovjak

Research output: Contribution to journalArticlepeer-review

62 Citations (Scopus)

Abstract

Optogenetics and photopharmacology enable the spatio-temporal control of cell and animal behavior by light. Although red light offers deep-tissue penetration and minimal phototoxicity, very few red-light-sensitive optogenetic methods are currently available. We have now developed a red-light-induced homodimerization domain. We first showed that an optimized sensory domain of the cyanobacterial phytochrome 1 can be expressed robustly and without cytotoxicity in human cells. We then applied this domain to induce the dimerization of two receptor tyrosine kinases - the fibroblast growth factor receptor 1 and the neurotrophin receptor trkB. This new optogenetic method was then used to activate the MAPK/ERK pathway non-invasively in mammalian tissue and in multicolor cell-signaling experiments. The light-controlled dimerizer and red-light-activated receptor tyrosine kinases will prove useful to regulate a variety of cellular processes with light. Go deep with red: The sensory domain (S) of the cyanobacterial phytochrome 1 (CPH1) was repurposed to induce the homodimerization of proteins in living cells by red light. By using this domain, light-activated protein kinases were engineered that can be activated orthogonally from many fluorescent proteins and through mammalian tissue. Pr/Pfr=red-/far-red-absorbing state of CPH1.

Original languageEnglish
Pages (from-to)6339-6342
Number of pages4
JournalAngewandte Chemie - International Edition
Volume55
Issue number21
DOIs
Publication statusPublished - 17 May 2016
Externally publishedYes

Keywords

  • optogenetics
  • photochromism
  • phytochrome
  • receptors

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