Pr-lynx1, a modulator of nicotinic acetylcholine receptors in the insect

Choo, Young Moo; Lee, Byung Hwan; Lee, Kwang-Sik; Kim, Bo Yeon; Li, Jianhong; Kim, Jong Gill; Lee, Jae Heon; Sohn, Hung Dae; Nah, Seung Yeol; Jin, Byung Rae

doi:10.1016/j.mcn.2008.02.011

Cited by 17 publications

(31 citation statements)

References 56 publications

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“…Recombinant baculoviruses were propagated in Sf9 cells cultured in TC100 medium (Gibco BRL) at 27°C. Recombinant proteins were purified using a HisTrap column (Amersham Biosciences) and injected into BALB/c mice to produce a polyclonal antibody [50]. The protein concentration was determined using the Bio-Rad Protein Assay Kit.…”

Section: Methodsmentioning

confidence: 99%

Dual Function of a Bee Venom Serine Protease: Prophenoloxidase-Activating Factor in Arthropods and Fibrin(ogen)olytic Enzyme in Mammals

et al. 2010

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Bee venom contains a variety of peptides and enzymes, including serine proteases. While the presence of serine proteases in bee venom has been demonstrated, the role of these proteins in bee venom has not been elucidated. Furthermore, there is currently no information available regarding the melanization response or the fibrin(ogen)olytic activity of bee venom serine protease, and the molecular mechanism of its action remains unknown. Here we show that bee venom serine protease (Bi-VSP) is a multifunctional enzyme. In insects, Bi-VSP acts as an arthropod prophenoloxidase (proPO)-activating factor (PPAF), thereby triggering the phenoloxidase (PO) cascade. Bi-VSP injected through the stinger induces a lethal melanization response in target insects by modulating the innate immune response. In mammals, Bi-VSP acts similarly to snake venom serine protease, which exhibits fibrin(ogen)olytic activity. Bi-VSP activates prothrombin and directly degrades fibrinogen into fibrin degradation products, defining roles for Bi-VSP as a prothrombin activator, a thrombin-like protease, and a plasmin-like protease. These findings provide a novel view of the mechanism of bee venom in which the bee venom serine protease kills target insects via a melanization strategy and exhibits fibrin(ogen)olytic activity.

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Section: Methodsmentioning

confidence: 99%

Dual Function of a Bee Venom Serine Protease: Prophenoloxidase-Activating Factor in Arthropods and Fibrin(ogen)olytic Enzyme in Mammals

et al. 2010

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“…As for in vivo application, blocking the inactivation of the voltage-gated Na + channel para in the fly’s circadian system clock neurons using a GPI-tethered d-ACTX-Hv1a toxin induces rhythmic action potential bursts and depolarised plateau potentials, causing circadian phase advancement (Wu et al ., 2008). Interestingly, Sleepless, a Ly-6/neurotoxin family member, is an endogenous regulator of Shaker K + channels (Wu et al ., 2010) while other members of the Ly-6 family are endogenous modulators for nAChR in insects and mammals (Choo et al ., 2008; Morishita et al ., 2010). Comparing RNAi and dominant-negative approaches, which intervene at the stages of channel synthesis and assembly, t-toxins directly bind and block channels and receptors after these are assembled, suggesting that they may have faster kinetics.…”

Section: Bridging Synaptophysiology To Structural Connectomicsmentioning

confidence: 99%

The Genetic Analysis of Functional Connectomics in Drosophila

Meinertzhagen

Lee

2012

Advances in Genetics

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Fly and vertebrate nervous systems share many organization characteristics, such as layers, columns and glomeruli, and utilize similar synaptic components, such ion channels and receptors. Both also exhibit similar network features. Recent technological advances, especially in electron microscopy, now allow us to determine synaptic circuits and identify pathways cell-by-cell, as part of the fly’s connectome. Genetic tools provide the means to identify synaptic components, as well as to record and manipulate neuronal activity, adding function to the connectome. This review discusses technical advances in these emerging areas of functional connectomics, offering prognoses in each and identifying the challenges in bridging structural connectomics to molecular biology and synaptic physiology, thereby determining fundamental computation mechanisms that underlie behaviour.

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“…Reflecting their differential expression, Ly6 proteins are used in diverse biological processes. Apart from acting as GPI-linked cell accessory proteins of the immune system, vertebrate Ly6 proteins function in the modulation of nicotinic acetylcholine receptors (Choo et al, 2008;Darvas et al, 2009;Grando, 2008;Levitin et al, 2008;Liu et al, 2009), remodelling of the extracellular matrix during skeletal muscle regeneration (Kafadar et al, 2009), self-renewal of erythroid progenitors (Bresson-Mazet et al, 2008), and lipolytic processing of triglyceride-rich lipoproteins by binding lipoprotein lipase (Beigneux et al, 2009). The presence of a GPI-anchor in Ly6 molecules, a lipid anchor that tethers the proteins on the outer leaflet of the membrane, also suggests that Ly6 proteins can aggregate in lipid rafts to alter the activity of associated proteins (Bamezai, 2004;Halova et al, 2002).…”

Section: Diverse Functions Of Ly6 Proteinsmentioning

confidence: 99%

Crooked, Coiled and Crimpled are three Ly6-like proteins required for proper localization of septate junction components

et al. 2010

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SUMMARYCellular junction formation is an elaborate process that is dependent on the regulated synthesis, assembly and membrane targeting of constituting components. Here, we report on three Drosophila Ly6-like proteins essential for septate junction (SJ) formation. SJs provide a paracellular diffusion barrier and appear molecularly and structurally similar to vertebrate paranodal septate junctions. We show that Crooked (Crok), a small GPI-anchored Ly6-like protein, is required for septa formation and barrier functions. In embryos that lack Crok, SJ components are produced but fail to accumulate at the plasma membrane. Crok is detected in intracellular puncta and acts tissue-autonomously, which suggests that it resides in intracellular vesicles to assist the cell surface localization of SJ components. In addition, we demonstrate that two related Ly6 proteins, Coiled (Cold) and Crimpled (Crim), are required for SJ formation and function in a tissue-autonomous manner, and that Cold also localizes to intracellular vesicles. Specifically, Crok and Cold are required for correct membrane trafficking of Neurexin IV, a central SJ component. The non-redundant requirement for Crok, Cold, Crim and Boudin (Bou; another Ly6 protein that was recently shown to be involved in SJ formation) suggests that members of this conserved family of proteins cooperate in the assembly of SJ components, possibly by promoting core SJ complex formation in intracellular compartments associated with membrane trafficking.

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Pr-lynx1, a modulator of nicotinic acetylcholine receptors in the insect

Cited by 17 publications

References 56 publications

Dual Function of a Bee Venom Serine Protease: Prophenoloxidase-Activating Factor in Arthropods and Fibrin(ogen)olytic Enzyme in Mammals

Dual Function of a Bee Venom Serine Protease: Prophenoloxidase-Activating Factor in Arthropods and Fibrin(ogen)olytic Enzyme in Mammals

The Genetic Analysis of Functional Connectomics in Drosophila

Crooked, Coiled and Crimpled are three Ly6-like proteins required for proper localization of septate junction components

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