The LOV Domain Family:  Photoresponsive Signaling Modules Coupled to Diverse Output Domains

Crosson, Sean; Rajagopal, Sudarshan; Moffat, Keith

doi:10.1021/bi026978l

Cited by 388 publications

(469 citation statements)

References 62 publications

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“…These data, although indirect, suggest that WC-1 has a long period photocycle (>1 h). This is likely due to the formation of long-lived photoactivated intermediate in its LOV domain, which involves the formation of a covalent bond between the critical and highly conserved cysteine residue of the LOV domain and the flavin chromophore (Salomon et al 2000;Crosson and Moffat 2002;Crosson et al 2003;Harper et al 2003). Such a photochemical characteristic of WC-1 will render most of the proteins incapable of being reactivated by light and will have a major impact on its function (see below).…”

Section: Long Period Photocycle Of Wc-1mentioning

confidence: 99%

Molecular mechanism of light responses in Neurospora: from light-induced transcription to photoadaptation

He¹,

Liu²

2005

Genes Dev.

190

239

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Section: Long Period Photocycle Of Wc-1mentioning

confidence: 99%

Molecular mechanism of light responses in Neurospora: from light-induced transcription to photoadaptation

He¹,

Liu²

2005

Genes Dev.

190

239

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“…21,22 Specifically, the side chain of a conserved glutamine residue within LOV2 (Gln 575 in Arabidopsis phot1) which forms hydrogen bonds with the FMN chromophore flips by 180° upon cysteinyl adduct formation 11,23,24 causing protein changes in the central b-sheet scaffold that forms contacts with the Ja-helix. 19,20 We have recently shown that mutation of the conserved glutamine to leucine (Q575L) attenuates light-induced autophosphorylation of Arabidopsis phot1 expressed in insect cells, 13 suggesting that this residue plays a role in transmitting the signal generated upon light-driven cysteinyl adduct formation from within LOV2 to protein changes at the LOV2 surface.…”

Section: Lov2 Signal Transmissionmentioning

confidence: 99%

Phototropin Receptor Kinase Activation by Blue Light

Jones

Christie

2008

Plant Signaling & Behavior

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Phototropins (phot1 and phot2) are blue light-activated serine/ threonine protein kinases that function to mediate a variety of adaptive processes that serve to optimize the photosynthetic efficiency of plants and thereby promote their growth. Light sensing by the phototropins is mediated by a repeated motif located within the N-terminal region of the protein designated the LOV domain. Although phototropins possess two LOV photosensors (LOV1 and LOV2), recent biophysical and structure-function analyses clearly indicate that the LOV2 domain plays a predominant role in regulating phototropin kinase activity owing to specific protein changes that occur in response to LOV2 photoexcitation. In particular, the central b-sheet scaffold plays a role in propagating the photochemical signal generated from within LOV2 to protein changes at the surface that are necessary for kinase activation. Light-Induced Activation of Phot1The primary amino acid structures of plant phototropins (phot1 and phot2) can be separated into two distinct regions: a N-terminal photosensory region linked to a C-terminal effector domain that includes a classic serine/threonine kinase motif. [1][2][3] The N-terminal photosensory region comprises two LOV domains each of which binds the blue light absorbing cofactor flavin mononucleotide (FMN) as chromophore. 4,5 LOV domains exhibit significant homology to motifs found in a diverse range of eukaryotic and prokaryotic proteins involved in sensing Light, Oxygen or Voltage, hence the acronym LOV. 6 Bacterially expressed LOV domains are photochemically reactive as monitored by absorbance spectroscopy. 7 In the dark, LOV domains bind FMN non-covalently forming a spectral species, LOV 447 , which absorbs maximally near 447 nm. 7,8 Irradiation of the domain induces the formation of a covalent bond between the C(4a) carbon of the FMN and the sulfur atom of a nearby, conserved cysteine residue within the domain. Cysteinyl adduct formation occurs within microseconds of illumination and produces a spectral species, LOV 390 , that absorbs maximally near 390 nm. 8 Mutation of the afore-mentioned active-site cysteine to either alanine or serine results in a loss of photochemical reactivity of the LOV domain. 7,8 Moreover, this mutation has been used successfully to probe the roles of LOV1 and LOV2 in regulating phototropin activity and function. [9][10][11][12] As reported previously (ref. 13), the Cys → Ala mutation within LOV2 of Arabidopsis thaliana phot1 (C517A) results in a loss of light-induced receptor autophosphorylation when expressed in insect cells (Fig. 1A), demonstrating that LOV2 is the principle photosensor regulating phot1 kinase activity. A similar mode of action has been reported for the LOV2 domain of Arabidopsis phot2. 12,14,15 The LOV1 domain, by contrast, is proposed to mediate receptor dimerization 16 and/or modulate the photoreactivity of LOV2. 14 Substitution of the conserved active-site cysteine with methionine has been shown to result in the formation of a unique photoproduct species abso...

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“…It was therefore concluded that phot1 and phot2 function redundantly as high light receptors, while phot1 acts as the low-light photoreceptor (Sakai et al, 2001). The phototropins are members of a larger family of sensor proteins known as the LOV domain family (Crosson et al, 2003). The family name is derived from the function of the LOV domain as a sensor for light, oxygen or voltage (Huala et al, 1997, Zhulin andTaylor, 1997;Taylor and Zhulin, 1999;Crosson et al, 2003).…”

Section: Saw the Lightmentioning

confidence: 99%

“…The phototropins are members of a larger family of sensor proteins known as the LOV domain family (Crosson et al, 2003). The family name is derived from the function of the LOV domain as a sensor for light, oxygen or voltage (Huala et al, 1997, Zhulin andTaylor, 1997;Taylor and Zhulin, 1999;Crosson et al, 2003). Each photoropin contains two LOV domains, termed LOV1 and LOV2 (Huala et al, 1997).…”

Section: Saw the Lightmentioning

confidence: 99%

“…Each photoropin contains two LOV domains, termed LOV1 and LOV2 (Huala et al, 1997). The non-phototropin members of the LOV family contain just a single LOV domain (Crosson et al, 2003). The phototreceptive properties of the photoropins is derived from the non-covalent binding of one flavin mononucleotide (FMN) molecule to each of its LOV domains (Christie et al, 1998; Figure 1).…”

Section: Saw the Lightmentioning

confidence: 99%

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Plant tropisms: providing the power of movement to a sessile organism

Esmon¹,

Pedmale²,

Liscum³

2005

Int. J. Dev. Biol.

108

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In an attempt to compensate for their sessile nature, plants have developed growth responses to deal with the copious and rapid changes in their environment. These responses are known as tropisms and they are marked by a directional growth response that is the result of differential cellular growth and development in response to an external stimulation such as light, gravity or touch. While the mechanics of tropic growth and subsequent development have been the topic of debate for more than a hundred years, only recently have researchers been able to make strides in understanding how plants perceive and respond to tropic stimulations, thanks in large part to mutant analysis and recent advances in genomics. This paper focuses on the recent advances in four of the best-understood tropic responses and how each affects plant growth and development: phototropism, gravitropism, thigmotropism and hydrotropism. While progress has been made in deciphering the events between tropic stimulation signal perception and each characteristic growth response, there are many areas that remain unclear, some of which will be discussed herein. As has become evident, each tropic response pathway exhibits distinguishing characteristics. However, these pathways of tropic perception and response also have overlapping components -a fact that is certainly related to the necessity for pathway integration given the everchanging environment that surrounds every plant.

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The LOV Domain Family: Photoresponsive Signaling Modules Coupled to Diverse Output Domains

Cited by 388 publications

References 62 publications

Molecular mechanism of light responses in Neurospora: from light-induced transcription to photoadaptation

Molecular mechanism of light responses in Neurospora: from light-induced transcription to photoadaptation

Phototropin Receptor Kinase Activation by Blue Light

Plant tropisms: providing the power of movement to a sessile organism

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