Research ExplorerPublicationsRhodopsin-cyclases for photocontrol of cGMP/cAMP and 2.3 Å s...

Rhodopsin-cyclases for photocontrol of cGMP/cAMP and 2.3 Å structure of the adenylyl cyclase domain

Standard

Rhodopsin-cyclases for photocontrol of cGMP/cAMP and 2.3 Å structure of the adenylyl cyclase domain. / Scheib, Ulrike; Broser, Matthias; Constantin, Oana M; Yang, Shang; Gao, Shiqiang; Mukherjee, Shatanik; Stehfest, Katja; Nagel, Georg; Gee, Christine E; Hegemann, Peter.

In: NAT COMMUN, Vol. 9, No. 1, 24.05.2018, p. 2046.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Scheib, U, Broser, M, Constantin, OM, Yang, S, Gao, S, Mukherjee, S, Stehfest, K, Nagel, G, Gee, CE & Hegemann, P 2018, 'Rhodopsin-cyclases for photocontrol of cGMP/cAMP and 2.3 Å structure of the adenylyl cyclase domain', NAT COMMUN, vol. 9, no. 1, pp. 2046. https://doi.org/10.1038/s41467-018-04428-w

APA

Scheib, U., Broser, M., Constantin, O. M., Yang, S., Gao, S., Mukherjee, S., Stehfest, K., Nagel, G., Gee, C. E., & Hegemann, P. (2018). Rhodopsin-cyclases for photocontrol of cGMP/cAMP and 2.3 Å structure of the adenylyl cyclase domain. NAT COMMUN, 9(1), 2046. https://doi.org/10.1038/s41467-018-04428-w

Vancouver

Scheib U, Broser M, Constantin OM, Yang S, Gao S, Mukherjee S et al. Rhodopsin-cyclases for photocontrol of cGMP/cAMP and 2.3 Å structure of the adenylyl cyclase domain. NAT COMMUN. 2018 May 24;9(1):2046. https://doi.org/10.1038/s41467-018-04428-w

Bibtex

@article{f46f21276ba645dda68aec35fb9149e3,
title = "Rhodopsin-cyclases for photocontrol of cGMP/cAMP and 2.3 {\AA} structure of the adenylyl cyclase domain",
abstract = "The cyclic nucleotides cAMP and cGMP are important second messengers that orchestrate fundamental cellular responses. Here, we present the characterization of the rhodopsin-guanylyl cyclase from Catenaria anguillulae (CaRhGC), which produces cGMP in response to green light with a light to dark activity ratio >1000. After light excitation the putative signaling state forms with τ = 31 ms and decays with τ = 570 ms. Mutations (up to 6) within the nucleotide binding site generate rhodopsin-adenylyl cyclases (CaRhACs) of which the double mutated YFP-CaRhAC (E497K/C566D) is the most suitable for rapid cAMP production in neurons. Furthermore, the crystal structure of the ligand-bound AC domain (2.25 {\AA}) reveals detailed information about the nucleotide binding mode within this recently discovered class of enzyme rhodopsin. Both YFP-CaRhGC and YFP-CaRhAC are favorable optogenetic tools for non-invasive, cell-selective, and spatio-temporally precise modulation of cAMP/cGMP with light.",
keywords = "Journal Article",
author = "Ulrike Scheib and Matthias Broser and Constantin, {Oana M} and Shang Yang and Shiqiang Gao and Shatanik Mukherjee and Katja Stehfest and Georg Nagel and Gee, {Christine E} and Peter Hegemann",
note = "I am co-senior author together with Peter Hegemann (Humboldt Uni) on this publication - we were equal contributors",
year = "2018",
month = may,
day = "24",
doi = "10.1038/s41467-018-04428-w",
language = "English",
volume = "9",
pages = "2046",
journal = "NAT COMMUN",
issn = "2041-1723",
publisher = "NATURE PUBLISHING GROUP",
number = "1",

}

RIS

TY - JOUR

T1 - Rhodopsin-cyclases for photocontrol of cGMP/cAMP and 2.3 Å structure of the adenylyl cyclase domain

AU - Scheib, Ulrike

AU - Broser, Matthias

AU - Constantin, Oana M

AU - Yang, Shang

AU - Gao, Shiqiang

AU - Mukherjee, Shatanik

AU - Stehfest, Katja

AU - Nagel, Georg

AU - Gee, Christine E

AU - Hegemann, Peter

N1 - I am co-senior author together with Peter Hegemann (Humboldt Uni) on this publication - we were equal contributors

PY - 2018/5/24

Y1 - 2018/5/24

N2 - The cyclic nucleotides cAMP and cGMP are important second messengers that orchestrate fundamental cellular responses. Here, we present the characterization of the rhodopsin-guanylyl cyclase from Catenaria anguillulae (CaRhGC), which produces cGMP in response to green light with a light to dark activity ratio >1000. After light excitation the putative signaling state forms with τ = 31 ms and decays with τ = 570 ms. Mutations (up to 6) within the nucleotide binding site generate rhodopsin-adenylyl cyclases (CaRhACs) of which the double mutated YFP-CaRhAC (E497K/C566D) is the most suitable for rapid cAMP production in neurons. Furthermore, the crystal structure of the ligand-bound AC domain (2.25 Å) reveals detailed information about the nucleotide binding mode within this recently discovered class of enzyme rhodopsin. Both YFP-CaRhGC and YFP-CaRhAC are favorable optogenetic tools for non-invasive, cell-selective, and spatio-temporally precise modulation of cAMP/cGMP with light.

AB - The cyclic nucleotides cAMP and cGMP are important second messengers that orchestrate fundamental cellular responses. Here, we present the characterization of the rhodopsin-guanylyl cyclase from Catenaria anguillulae (CaRhGC), which produces cGMP in response to green light with a light to dark activity ratio >1000. After light excitation the putative signaling state forms with τ = 31 ms and decays with τ = 570 ms. Mutations (up to 6) within the nucleotide binding site generate rhodopsin-adenylyl cyclases (CaRhACs) of which the double mutated YFP-CaRhAC (E497K/C566D) is the most suitable for rapid cAMP production in neurons. Furthermore, the crystal structure of the ligand-bound AC domain (2.25 Å) reveals detailed information about the nucleotide binding mode within this recently discovered class of enzyme rhodopsin. Both YFP-CaRhGC and YFP-CaRhAC are favorable optogenetic tools for non-invasive, cell-selective, and spatio-temporally precise modulation of cAMP/cGMP with light.

KW - Journal Article

U2 - 10.1038/s41467-018-04428-w

DO - 10.1038/s41467-018-04428-w

M3 - SCORING: Journal article

C2 - 29799525

VL - 9

SP - 2046

JO - NAT COMMUN

JF - NAT COMMUN

SN - 2041-1723

IS - 1

ER -