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Engineering of a red-light-activated human cAMP/cGMP-specific phosphodiesterase

Title data

Gasser, Carlos ; Taiber, Sandra ; Yeh, Chen-Min ; Wittig, Charlotte Helene ; Hegemann, Peter ; Ryu, Soojin ; Wunder, Frank ; Möglich, Andreas:
Engineering of a red-light-activated human cAMP/cGMP-specific phosphodiesterase.
In: Proceedings of the National Academy of Sciences of the United States of America. Vol. 111 (17 June 2014) Issue 24 . - pp. 8803-8808.
ISSN 1091-6490
DOI: https://doi.org/10.1073/pnas.1321600111

Project information

Project financing: Alexander von Humboldt-Stiftung
DFG
Max-Planck-Gesellschaft

Abstract in another language

Sensory photoreceptors elicit vital physiological adaptations in response to incident light. As light-regulated actuators, photoreceptors underpin optogenetics, which denotes the noninvasive, reversible, and spatiotemporally precise perturbation by light of living cells and organisms. Of particular versatility, naturally occurring photoactivated adenylate cyclases promote the synthesis of the second messenger cAMP under blue light. Here, we have engineered a light-activated phosphodiesterase (LAPD) with complementary light sensitivity and catalytic activity by recombining the photosensor module of Deinococcus radiodurans bacterial phytochrome with the effector module of Homo sapiens phosphodiesterase 2A. Upon red-light absorption, LAPD up-regulates hydrolysis of cAMP and cGMP by up to sixfold, whereas far-red light can be used to down-regulate activity. LAPD also mediates light-activated cAMP and cGMP hydrolysis in eukaryotic cell cultures and in zebrafish embryos; crucially, the biliverdin chromophore of LAPD is available endogenously and does not need to be provided exogenously. LAPD thus establishes a new optogenetic modality that permits light control over diverse cAMP/cGMP-mediated physiological processes. Because red light penetrates tissue more deeply than light of shorter wavelengths, LAPD appears particularly attractive for studies in living organisms.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 24051046
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Andreas Möglich
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Professorship Biochemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry
Result of work at the UBT: No
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 19 May 2015 06:42
Last Modified: 19 May 2015 06:42
URI: https://eref.uni-bayreuth.de/id/eprint/13592