Cooperative functions of the two F-BAR proteins Cip4 and Nostrin in regulating E-cadherin in epithelial morphogenesis

Zobel, Thomas; Brinkmann, Klaus; Koch, Nicole; Schneider, Katharina; Seemann, Eric; Fleige, Astrid; Qualmann, Britta; Kessels, Michael M.; Bogdan, Sven

doi:10.1242/jcs.155929

Cited by 22 publications

(21 citation statements)

References 73 publications

(110 reference statements)

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“…In line with this notion, it has been shown that NOSTRIN localizes to rab11-positive (and to a lesser extend rab5-positive) endosomes and might function at endosomal tubule intermediates to mediate microtubuledependent trafficking of recycling endosomes. 56 We originally identified NOSTRIN as an eNOS interaction partner 21 and established its function as an adaptor for eNOS, dynamin, neuronal Wiskott-Aldrich Syndrome protein, and caveolin that affected the subcellular localization of eNOS. 21,29,31 However, the role of NOSTRIN in regulating NO production in vivo and its role in pathophysiology were unclear.…”

Section: Discussionmentioning

confidence: 99%

The F-BAR Protein NOSTRIN Dictates the Localization of the Muscarinic M3 Receptor and Regulates Cardiovascular Function

Kovačević

Müller

Kojonazarov

et al. 2015

Circulation Research

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Rationale: Endothelial dysfunction is an early event in cardiovascular disease and characterized by reduced production of nitric oxide (NO). The F-BAR protein NO synthase traffic inducer (NOSTRIN) is an interaction partner of endothelial NO synthase and modulates its subcellular localization, but the role of NOSTRIN in pathophysiology in vivo is unclear. Objective: We analyzed the consequences of deleting the NOSTRIN gene in endothelial cells on NO production and cardiovascular function in vivo using NOSTRIN knockout mice. Methods and Results: The levels of NO and cGMP were significantly reduced in mice with endothelial cell–specific deletion of the NOSTRIN gene resulting in diastolic heart dysfunction. In addition, systemic blood pressure was increased, and myograph measurements indicated an impaired acetylcholine-induced relaxation of isolated aortic rings and resistance arteries. We found that the muscarinic acetylcholine receptor subtype M3 (M3R) interacted directly with NOSTRIN, and the latter was necessary for correct localization of the M3R at the plasma membrane in murine aorta. In the absence of NOSTRIN, the acetylcholine-induced increase in intracellular Ca 2+ in primary endothelial cells was abolished. Moreover, the activating phosphorylation and Golgi translocation of endothelial NO synthase in response to the M3R agonist carbachol were diminished. Conclusions: NOSTRIN is crucial for the localization and function of the M3R and NO production. The loss of NOSTRIN in mice leads to endothelial dysfunction, increased blood pressure, and diastolic heart failure.

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Section: Discussionmentioning

confidence: 99%

The F-BAR Protein NOSTRIN Dictates the Localization of the Muscarinic M3 Receptor and Regulates Cardiovascular Function

Kovačević

Müller

Kojonazarov

et al. 2015

Circulation Research

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“…Cip4::YFP (PBac{754.P.FSVS-0}Cip4 CPTI003231 , Kyoto Stock Center); hsFLP/TM6 (Bloomington Drosophila Stock Center, #279); lmd 1 /TM3, Kr>>lacZ (Duan et al 2001); (Zobel et al 2015); Nost df004 (this work); Nost ff016 (this work); Nost df004 ;;Cip4 Δ32 ,Synd 1d /TM3, twi>>GFP (this work); Nost df004 ;;Cip4 Δ32 , Synd dEx22 /TM3, twi>>GFP (this work); Nost df004 ;;Cip4 Δ32 /TM3,hs-hid3 (Zobel et al 2015)(and this work); Nost df004 ;;Cip4 Δ32 /TM3, twi>>GFP (this work); Nost df004 ;;Synd 1d /TM3, twi>>GFP (this work); Nost df004 ;;Synd dEx22 /TM3,twi>>GFP (this work); P{XP}CG10962 d08142 (Harvard Medical School); PBac{WH}CG10962 f02373 (Harvard Medical School); PBac{WH}f06363 (Harvard Medical School); rP289-lacZ (Nose et al 1998); Synd 1d /TM3,twi>>GFP (Kumar et al 2009b); Synd dEx22 /TM3,twi>>GFP (Kumar et al 2009a); Mef2-GAL4 (Ranganayakulu et al 1998).…”

Section: Drosophila Strainsmentioning

confidence: 99%

“…To obtain adult flies homozygous mutant for both Nostrin and Cip4 (lacking the zygotic and maternal expression of both genes) the strain Nost df004 ;;Cip4 Δ32 /TM3,hs-hid3 (see also Zobel et al 2015) was used. Heat shocking the progeny for 1,5 hours at 37°C during 3 -4 days resulted in the survival of only homozygous double mutant escaper flies and the death of all animals carrying the balancer chromosome.…”

Section: Generation Of Homozygous Nostrin and Cip4 And Of Cip4 Syndapmentioning

confidence: 99%

“…Here we focus on the analysis of Drosophila Nostrin and two related genes, Cip4 and Syndapin (Synd), within this superfamily that encode F-BAR plus SH3 domain proteins, during muscle development. Previously, the functions of these Drosophila genes have been characterized within other developmental contexts, including germ line cell encapsulation (Nost; Zobel et al 2015), the formation of proper numbers of wing hairs (Cip4; Fricke et al 2009), and postsynaptic membrane organization (Synd; Kumar et al 2009b). As described herein, our genetic analysis of these F-BAR genes in Drosophila muscle development shows that their encoded proteins, particularly Nostrin and Cip4, make joint contributions to myoblast fusion during embryogenesis.…”

Section: Introductionmentioning

confidence: 99%

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RNAi screen inTriboliumreveals involvement of F-BAR proteins in myoblast fusion and visceral muscle morphogenesis in insects

Schultheis

Schwirz

Frasch

2018

Preprint

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In a large-scale RNAi screen in Tribolium castaneum for genes with knock-down phenotypes in the larval somatic musculature, one recurring phenotype was the appearance of larval muscle fibers that were significantly thinner than those in control animals. Several of the genes producing this knock-down phenotype corresponded to orthologs of Drosophila genes that are known to participate in myoblast fusion, particularly via their effects on actin polymerization. A new gene previously not implicated in myoblast fusion but displaying a similar thin-muscle knock-down phenotype was the Tribolium ortholog of Nostrin, which encodes an F-BAR and SH3 domain protein. Our genetic studies of Nostrin and Cip4, a gene encoding a structurally related protein, in Drosophila show that the encoded F-BAR proteins jointly contribute to efficient myoblast fusion during larval muscle development. In addition, they are required during the profound remodeling of the midgut visceral musculature during metamorphosis, which we also portray. We propose that these F-Bar proteins help govern proper morphogenesis particularly of the longitudinal midgut muscles during metamorphosis.

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“…Rabbits were immunized with purified proteins (Davids Biotechnologie, Regensburg, Germany). Affinity purification was done as described previously (Zobel et al, 2015).…”

Section: Cell Culture Cell Transfection and Pulldown Experimentsmentioning

confidence: 99%

WHAMY is a novel actin polymerase promoting myoblast fusion, macrophage cell motility and sensory organ development in Drosophila

Brinkmann

Winterhoff

Önel

et al. 2016

Journal of Cell Science

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Wiskott-Aldrich syndrome proteins (WASPs) are nucleationpromoting factors (NPF) that differentially control the Arp2/3 complex. In Drosophila, three different family members, SCAR (also known as WAVE), WASP and WASH (also known as CG13176), have been analyzed so far. Here, we characterized WHAMY, the fourth Drosophila WASP family member. whamy originated from a wasp gene duplication and underwent a sub-neofunctionalization. Unlike WASP, we found that WHAMY specifically interacted with activated Rac1 through its two CRIB domains, which were sufficient for targeting WHAMY to lamellipodial and filopodial tips. Biochemical analyses showed that WHAMY promoted exceptionally fast actin filament elongation, although it did not activate the Arp2/3 complex. Loss-and gain-of-function studies revealed an important function of WHAMY in membrane protrusions and cell migration in macrophages. Genetic data further implied synergistic functions between WHAMY and WASP during morphogenesis. Double mutants were late-embryonic lethal and showed severe defects in myoblast fusion. Trans-heterozygous mutant animals showed strongly increased defects in sensory cell fate specification. Thus, WHAMY is a novel actin polymerase with an initial partitioning of ancestral WASP functions in development and subsequent acquisition of a new function in cell motility during evolution.

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Cooperative functions of the two F-BAR proteins Cip4 and Nostrin in regulating E-cadherin in epithelial morphogenesis

Cited by 22 publications

References 73 publications

The F-BAR Protein NOSTRIN Dictates the Localization of the Muscarinic M3 Receptor and Regulates Cardiovascular Function

The F-BAR Protein NOSTRIN Dictates the Localization of the Muscarinic M3 Receptor and Regulates Cardiovascular Function

RNAi screen inTriboliumreveals involvement of F-BAR proteins in myoblast fusion and visceral muscle morphogenesis in insects

WHAMY is a novel actin polymerase promoting myoblast fusion, macrophage cell motility and sensory organ development in Drosophila

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