Light-regulated interaction of Dmoesin with TRP and TRPL channels is required for maintenance of photoreceptors

Chorna-Ornan, Irit; Tzarfaty, Vered; Ankri-Eliahoo, Galit; Joel-Almagor, Tamar; Meyer, Nina; Huber, Armin; Payre, François; Minke, Baruch

doi:10.1083/jcb.200503014

Cited by 43 publications

(36 citation statements)

References 39 publications

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“…The recently characterized phosphoprotein retinophilin, which is required to suppress photoreceptor dark noise, becomes dephosphorylated when the flies are kept in the light (50). Another example for light-dependent dephosphorylation is Drosophila dMoesin (51). Here, dephosphorylation regulates the interaction of dMoesin with TRP and TRPL ion channels and its migration from the membrane to the cytoplasm.…”

Section: Discussionmentioning

confidence: 99%

Light-dependent Phosphorylation of the Drosophila Transient Receptor Potential Ion Channel

Voolstra

Beck

Oberegelsbacher

et al. 2010

Journal of Biological Chemistry

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Reversible protein phosphorylation is a well established mechanism for regulating the activity of ion channels. Typically, the pattern of phosphorylation of ion channels is complex, involving several phosphorylation sites with consensus sequences for a number of protein kinases, such as protein kinase C (PKC), 3 protein kinase A, calcium/calmodulin-dependent protein kinase, or casein kinase, which phosphorylate serine and threonine residues, as well as kinases phosphorylating tyrosine residues. For example, in the major delayed rectifier K ϩ channel Kv2.1, expressed in most central neurons, 16 phosphorylation sites have been identified by mass spectrometry, a subset of which contributes to graded modulation of voltagedependent gating (2).Transient receptor potential (TRP) channels constitute a protein family of about 30 unique homologs that are assigned to seven subfamilies on the basis of sequence homology: canonical TRPC, vanilloid TRPV, melastatin TRPM, polycystin TRPP, mucolipin TRPML, and ankyrin transmembrane proteins TRPA and NOMPC-like TRPN (3, 4). The founding member of this protein family is the Drosophila TRP channel, which, together with its homolog TRP-like (TRPL), is located in the rhabdomeral photoreceptor membrane of the fly compound eye and represents the major light-sensitive ion channel in this phospholipase C-mediated visual transduction cascade (5). Phosphorylation of several TRP channels has been described. Among the vertebrate TRPC channels, TRPC3 and TRPC6 are inhibited by phosphorylation events mediated by protein kinase C and protein kinase G (6 -8). In contrast, Src kinase activity is required for the activation of TRPC3 by diacylglycerol (9), and Fyn kinase phosphorylates and thereby increases the activity of TRPC6 (10). Abolition of the putative protein kinase C phosphorylation site Thr 635 in the S4/S5 linker region of TRPC3 by mutation results in increased channel activity and was found to underlie the phenotype of moonwalker mice, which is caused by loss of Purkinje cells (11). The regulation of the capsaicin-and heat-sensitive TRPV1 channel through phosphorylation of serine residues by protein kinase C is also well established (12)(13)(14). Phosphorylation of TRPV1 sensitizes this channel to capsaicin, heat, and other agonists. Besides protein kinase C, calcium/calmodulin-dependent kinase and protein kinase A were implicated in phosphorylation of TRPV1 (15, 16).The first TRP channel shown to become phosphorylated again was the Drosophila TRP channel. This channel is part of a signaling complex assembled by the INAD scaffold protein together with phospholipase C and an eye-enriched protein kinase C (eye-PKC) encoded by the inaC gene. It was shown initially for the larger fly Calliphora vicina and later also for Drosophila that the addition of ATP to the isolated signaling complex resulted in phosphorylation of TRP and INAD, suggesting that these two proteins of the signaling complex are targets of the associated protein kinase C (17)(18)(19)

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Section: Discussionmentioning

confidence: 99%

Light-dependent Phosphorylation of the Drosophila Transient Receptor Potential Ion Channel

Voolstra

Beck

Oberegelsbacher

et al. 2010

Journal of Biological Chemistry

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“…Fig.2A demonstrates that antibodies against non-phosphorylated and phosphorylated ERM proteins (anti-ERM; anti-pERM) identify, in the salivary gland, a single protein of ~75kDa corresponding well to the molecular mass of Drosophila moesin (Chorna-Ornan et al, 2005). These antibodies are directed against a peptide in the F-actinbinding site that is highly conserved between vertebrate ERM members and Drosophila moesin and that contains the Thr for phosphorylation (Polesello et al, 2002).…”

Section: Enrichment Of Phosphorylated Moesin At the Apical Plasma Memmentioning

confidence: 98%

Development of apical membrane organization and V-ATPase regulation in blowfly salivary glands

Baumann

Bauer

2013

Journal of Experimental Biology

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“…Studies of ERM function in the rhabdomere, the expanded light-sensitive apical surface of the Drosophila photoreceptor, also suggest that there is a dynamic role for ERMs in functional apical membrane elaboration (Chorna-Ornan et al, 2005;Karagiosis and Ready, 2004). The rhabdomere is a microvillusdense membrane that forms through the periscopic extension and 90-degree rotation of the photoreceptor apical membrane; the amplified membrane houses the light-sensitive signaling apparatus and holds it perpendicular to incoming light.…”

Section: Apical Elaborationmentioning

confidence: 99%

ERM proteins at a glance

McClatchey

2014

Journal of Cell Science

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The cell cortex is a dynamic and heterogeneous structure that governs cell identity and behavior. The ERM proteins (ezrin, radixin and moesin) are major architects of the cell cortex, and they link plasma membrane phospholipids and proteins to the underlying cortical actin cytoskeleton. Recent studies in several model systems have uncovered surprisingly dynamic and complex molecular activities of the ERM proteins and have provided new mechanistic insight into how they build and maintain cortical domains. Among many well-established and essential functions of ERM proteins, this Cell Science at a Glance article and accompanying poster will focus on the role of ERMs in organizing the cell cortex during cell division and apical morphogenesis. These examples highlight an emerging appreciation that the ERM proteins both locally alter the mechanical properties of the cell cortex, and control the spatial distribution and activity of key membrane complexes, establishing the ERM proteins as a nexus for the physical and functional organization of the cell cortex and making it clear that they are much more than scaffolds.This article is part of a Minifocus on Establishing polarity. For further reading, please see related articles: 'Establishment of epithelial polarity -GEF who's minding the GAP?' by Siu Ngok et al. (J. Cell Sci. 127,(3205)(3206)(3207)(3208)(3209)(3210)(3211)(3212)(3213)(3214)(3215). 'Integrins and epithelial cell polarity' by Jessica Lee and Charles Streuli (J. Cell Sci. 127, 3217-3225).

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Light-regulated interaction of Dmoesin with TRP and TRPL channels is required for maintenance of photoreceptors

Cited by 43 publications

References 39 publications

Light-dependent Phosphorylation of the Drosophila Transient Receptor Potential Ion Channel

Light-dependent Phosphorylation of the Drosophila Transient Receptor Potential Ion Channel

Development of apical membrane organization and V-ATPase regulation in blowfly salivary glands

ERM proteins at a glance

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