A Phytochrome Sensory Domain Permits Receptor Activation by Red Light. Issue 21 (21st April 2016)

• Record Type: Journal Article
• Authors: Reichhart, Eva; Ingles‐Prieto, Alvaro; Tichy, Alexandra‐Madelaine; McKenzie, Catherine; Janovjak, Harald
• Is Part Of: Angewandte Chemie international edition. Volume 55:Issue 21(2016)
• Page Start: 6339
• Page End: 6342
• Publication Date: 2016-04-21
• Subjects: optogenetics -- photochromism -- phytochrome -- receptors; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201601736
• Languages: English
• ISSNs: 1433-7851

Abstract

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. Abstract : 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.