Light-oxygen-voltage-sensing domain

Common to all LOV proteins is the blue-light sensitive flavin chromophore, which in the signaling state is covalently linked to the protein core via an adjacent cysteine residue. LOV domains are e.g. encountered in phototropins, which are blue-light-sensitive protein complexes regulating a great diversity of biological processes in higher plants as well as in micro-algae.{{cite journal |last1=Veetil |first1=S.K |last2=Mittal |first2=C |last3=Ranjan |first3=P |last4=Kateriya |first4=S |title=A conserved isoleucine in the LOV1 domain of a novel phototropin from the marine alga Ostreococcus tauri modulates the dark state recovery of the domain |journal=Biochim Biophys Acta |date=July 2011 |volume=1810 |issue=7 |pages=675–82 |doi=10.1016/j.bbagen.2011.04.008 |pmid=21554927 |url=https://www.sciencedirect.com/science/article/pii/S0304416511000857|url-access=subscription }} Phototropins are composed of two LOV domains, each containing a non-covalently bound flavin mononucleotide (FMN) chromophore in its dark-state form, and a C-terminal Ser-Thr kinase.

Upon blue-light absorption, a covalent bond between the FMN chromophore and an adjacent reactive cysteine residue of the apo-protein is formed in the LOV2 domain. This subsequently mediates the activation of the kinase, which induces a signal in the organism through phototropin autophosphorylation.

While the photochemical reactivity of the LOV2 domain has been found to be essential for the activation of the kinase, the in vivo functionality of the LOV1 domain within the protein complex still remains unclear.

In case of the fungus Neurospora crassa, the circadian clock is controlled by two light-sensitive domains, known as the white-collar-complex (WCC) and the LOV domain vivid (VVD-LOV). WCC is primarily responsible for the light-induced transcription on the control-gene frequency (FRQ) under day-light conditions, which drives the expression of VVD-LOV and governs the negative feedback loop onto the circadian clock. By contrast, the role of VVD-LOV is mainly modulatory and does not directly affect FRQ.

LOV domains have been found to control gene expression through DNA binding and

to be involved in redox-dependent regulation, like e.g. in the bacterium Rhodobacter sphaeroides. Notably, LOV-based optogenetic tools {{cite journal | vauthors = Wittmann T, Dema A, van Haren J| title = Lights, cytoskeleton, action: Optogenetic control of cell dynamics | date = May 2020 |publisher = Elsevier Ltd. | doi = 10.1016/j.ceb.2020.03.003| journal = Current Opinion in Cell Biology | volume = 66 | pages = 1–10 | pmid = 32371345 | pmc = 7577957 | doi-access = free }} have been gaining wide popularity in recent years to control a myriad of cellular events, including cell motility,{{Cite journal|title = A genetically encoded photoactivatable Rac controls the motility of living cells|journal = Nature|date = 2009-01-01|pmc = 2766670|pmid = 19693014|volume = 461|issue = 7260|pages = 104–8|doi = 10.1038/nature08241|first1 = Yi I.|last1 = Wu|first2 = Daniel|last2 = Frey|first3 = Oana I.|last3 = Lungu|first4 = Angelika|last4 = Jaehrig|first5 = Ilme|last5 = Schlichting |authorlink5=Ilme Schlichting |first6 = Brian|last6 = Kuhlman|first7 = Klaus M.|last7 = Hahn|bibcode = 2009Natur.461..104W}} subcellular organelle distribution,{{Cite journal|title = Optogenetic control of organelle transport and positioning|journal = Nature|date = 2015-01-01|volume = 518|issue = 7537|pages = 111–4|doi = 10.1038/nature14128|pmid = 25561173|first1 = Petra|last1 = van Bergeijk|first2 = Max|last2 = Adrian|first3 = Casper C.|last3 = Hoogenraad|first4 = Lukas C.|last4 = Kapitein|pmc=5063096|bibcode = 2015Natur.518..111V}} formation of membrane contact sites,{{Cite journal|title = Proteomic mapping of ER–PM junctions identifies STIMATE as a regulator of Ca²⁺ influx|journal = Nature Cell Biology|volume = 17|issue = 10|pages = 1339–47|date = 2015-01-01|doi = 10.1038/ncb3234|pmid = 26322679|first1 = Ji|last1 = Jing|first2 = Lian|last2 = He|first3 = Aomin|last3 = Sun|first4 = Ariel|last4 = Quintana|first5 = Yuehe|last5 = Ding|first6 = Guolin|last6 = Ma|first7 = Peng|last7 = Tan|first8 = Xiaowen|last8 = Liang|first9 = Xiaolu|last9 = Zheng|pmc=4589512}} microtubule dynamics,{{cite journal | vauthors = van Haren J, Charafeddine RA, Ettinger A, Wang H, Hahn KM, Wittmann T| title = Local control of intracellular microtubule dynamics by EB1 photodissociation | date = Mar 2018 |publisher = Nature Research. | doi = 10.1038/s41556-017-0028-5| journal = Nature Cell Biology| volume = 20 | issue = 3 | pages = 252–261 | pmid = 29379139 | pmc = 5826794 }} transcription,{{Cite journal|last1=Baaske|first1=Julia|last2=Gonschorek|first2=Patrick|last3=Engesser|first3=Raphael|last4=Dominguez-Monedero|first4=Alazne|last5=Raute|first5=Katrin|last6=Fischbach|first6=Patrick|last7=Müller|first7=Konrad|last8=Cachat|first8=Elise|last9=Schamel|first9=Wolfgang W. A.|last10=Minguet|first10=Susana|last11=Davies|first11=Jamie A.|date=2018-10-09|title=Dual-controlled optogenetic system for the rapid down-regulation of protein levels in mammalian cells|journal=Scientific Reports|volume=8|issue=1|pages=15024|doi=10.1038/s41598-018-32929-7|pmid=30301909|pmc=6177421|bibcode=2018NatSR...815024B|issn=2045-2322}} and protein degradation.{{Cite journal|title = A LOV2 Domain-Based Optogenetic Tool to Control Protein Degradation and Cellular Function|journal = Chemistry & Biology|issn = 1074-5521|pmid = 23601651|pages = 619–626|volume = 20|issue = 4|doi = 10.1016/j.chembiol.2013.03.005|first1 = Christian|last1 = Renicke|first2 = Daniel|last2 = Schuster|first3 = Svetlana|last3 = Usherenko|first4 = Lars-Oliver|last4 = Essen|first5 = Christof|last5 = Taxis|year = 2013|doi-access = free}}

• FMN-binding fluorescent proteins

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}}

{{Protein domains}}

Category:Sensory receptors

Category:Signal transduction

Category:Molecular biology

Category:Plant physiology