Downstream of Identity Genes: Muscle-Type-Specific Regulation of the Fusion Process

Bataillé, Laetitia; Delon, Isabelle; Ponte, Jean Philippe Da; Brown, Nicholas H.; Jagla, Krzysztof

doi:10.1016/j.devcel.2010.07.008

Cited by 53 publications

(51 citation statements)

References 46 publications

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“…3F-H,N-P; data not shown), demonstrating that T384 is not involved in protein interactions that mediate localization of ILK. This suggests that paxillin does not contribute to the localization of ILK in MASs, in agreement with the recent finding that functional MASs are formed in the absence of paxillin (Bataillé et al, 2010).…”

Section: Regions Of Ilk Required For Localization At Masssupporting

confidence: 79%

A central multifunctional role of integrin-linked kinase at muscle attachment sites

Zervas

Psarra

Williams

et al. 2011

Journal of Cell Science

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SummaryIntegrin-linked kinase (ILK) is an essential component of a multiprotein complex that links actin to the plasma membrane. Here, we have used a genetic approach to examine the molecular interactions that are essential for the assembly of this ILK-containing complex at Drosophila muscle attachment sites (MASs). We show that, downstream of integrins, talin plays a decisive role in the recruitment of three proteins: ILK, PINCH and paxillin. The accumulation of ILK at MASs appears to follow an amplification mechanism, suggesting that numerous binding sites are generated by minimal levels of the upstream integrin and talin effectors. This property suggests that ILK functions as an essential hub in the assembly of its partner proteins at sites of integrin adhesion. We found that PINCH stability, and its subcellular localization at MASs, depends upon ILK function, but that ILK stability and localization is not dependent upon PINCH. An in vivo structure-function analysis of ILK demonstrated that each ILK domain has sufficient information for its independent recruitment at embryonic MASs, whereas at later developmental stages only the kinase domain was effectively recruited. Our data strengthen the view that the ILK complex is assembled sequentially at sites of integrin adhesion by employing multiple molecular interactions, which collectively stabilize the integrin-actin link.

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Section: Regions Of Ilk Required For Localization At Masssupporting

confidence: 79%

A central multifunctional role of integrin-linked kinase at muscle attachment sites

Zervas

Psarra

Williams

et al. 2011

Journal of Cell Science

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“…Drosophila melanogaster stocks used in this study: Mef2::Gal4 , Act5C::Gal4 , UAS::GFP-Lamp1 , UAS::eGFP-huLC3 , UAS::myr-GFP , UAS::mito-GFP (all sourced from the Bloomington Drosophila Stock Center, Indiana University); ΔVinc, βPS-GFP , GFP-talin (all Klapholz et al, 2015); mys XG43 (Jannuzi et al, 2002); pax Δ1 (Bataille et al, 2010); talin-mCherry (Venken et al, 2011); UAS::talin (Tanentzapf et al, 2006); UAS::GFP-IBS2 (Ellis et al, 2011); paxillin-GFP (Bataille et al, 2010); UAS::paxillin (Vakaloglou et al, 2012); tensin-GFP (Torgler et al, 2004); ILK-YFP (unpublished, made as ILK-GFP in Zervas et al, 2001); PINCH-GFP (Kadrmas et al, 2004); Fermitin1-GFP (a genomic fragment, −1579 to +3942 relative to the ATG, with mGFP6 inserted following residue 228 and with three-serine linkers on each side; a gift of Danelle Devenport, The Gurdon Institute, University of Cambridge, UK). To misexpress vinculin constructs, the UAS-Gal4 system was used (Brand and Perrimon, 1993).…”

Section: Methodsmentioning

confidence: 99%

Drosophila vinculin is more harmful when hyperactive than absent, and can circumvent integrin to form adhesion complexes

Maartens

Wellmann

Wictome

et al. 2016

Journal of Cell Science

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Vinculin is a highly conserved protein involved in cell adhesion and mechanotransduction, and both gain and loss of its activity causes defective cell behaviour. Here, we examine how altering vinculin activity perturbs integrin function within the context of Drosophila development. Whereas loss of vinculin produced relatively minor phenotypes, gain of vinculin activity, through a loss of head–tail autoinhibition, caused lethality. The minimal domain capable of inducing lethality is the talin-binding D1 domain, and this appears to require talin-binding activity, as lethality was suppressed by competition with single vinculin-binding sites from talin. Activated Drosophila vinculin triggered the formation of cytoplasmic adhesion complexes through the rod of talin, but independently of integrin. These complexes contain a subset of adhesion proteins but no longer link the membrane to actin. The negative effects of hyperactive vinculin were segregated into morphogenetic defects caused by its whole head domain and lethality caused by its D1 domain. These findings demonstrate the crucial importance of the tight control of the activity of vinculin.

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“…Gain and loss-of-function experiments in D . melanogaster [9, 10] and C . elegans [11] embryos have identified roles for Paxillin orthologs in cytoskeletal organization required for morphogenesis and function of epithelia and muscles.…”

Section: Introductionmentioning

confidence: 99%

Evolution and Expression of Paxillin Genes in Teleost Fish

2016

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BackgroundPaxillin family proteins regulate intracellular signaling downstream of extracellular matrix adhesion. Tissue expression patterns and cellular functions of Paxillin proteins during embryo development remain poorly understood. Additionally, the evolution of this gene family has not been thoroughly investigated.ResultsThis report characterizes the evolution and expression of a novel Paxillin gene, called Paxillin-b, in Teleosts. Alignments indicate that Teleost Paxillin-a and Paxillin-b proteins are highly homologous to each other and to human Paxillin. Phylogenetic and synteny analyses suggest that these genes originated from the duplication of an ancestral Paxillin gene that was in a common ancestor of Teleosts and Tetrapods. Analysis of the spatiotemporal expression profiles of Paxillin-a and Paxillin-b using zebrafish revealed both overlapping and distinct domains for Paxillin-a and Paxillin-b during embryo development. Localization of zebrafish Paxillin orthologs expressed in mammalian cells demonstrated that both proteins localize to focal adhesions, similar to mammalian Paxillin. This suggests these proteins regulate adhesion-dependent processes in their endogenous tissues.ConclusionPaxillin-a and Paxillin-b were generated by duplication in Teleosts. These genes likely play similar roles as Paxillin genes in other organisms. This work provides a framework for functional investigation of Paxillin family members during development using the zebrafish as an in vivo model system.

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Downstream of Identity Genes: Muscle-Type-Specific Regulation of the Fusion Process

Cited by 53 publications

References 46 publications

A central multifunctional role of integrin-linked kinase at muscle attachment sites

A central multifunctional role of integrin-linked kinase at muscle attachment sites

Drosophila vinculin is more harmful when hyperactive than absent, and can circumvent integrin to form adhesion complexes

Evolution and Expression of Paxillin Genes in Teleost Fish

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