Passage of 17kDa calmodulin through gap junctions of three vertebrate species

Curran, Jennifer; Woodruff, Richard I.

doi:10.1016/j.tice.2007.06.002

Cited by 11 publications

(5 citation statements)

References 55 publications

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“…Furthermore, it was suggested that CaM might play a role in regulating endocytosis of Vgs ( Zhang et al 1994 ). These speculations were then proven correct when it was demonstrated that CaM, despite its large size of 17 kDa, and presumably because of its elongate shape ( Babu et al 1988 ), could pass through insect gap junctions ( Brooks et al 2004 ; Woodruff 2005 ; Cieniewicz et al 2008 ) as well as those of some vertebrates ( Curran et al 2007 ; Cieniewicz et al 2009 ). Additionally, in D. melanogaster it has been shown genetically by use of null-mutant germ-line cells that there is little or no CaM produced in the oocyte, and that the source of most or all of oocyte CaM is from the ovarian follicle epithelial cells ( Andruss et al 2004 ).…”

Section: Discussionmentioning

confidence: 99%

Vitellogenesis in the Fruit Fly,Drosophila melanogaster:Antagonists Demonstrate that the PLC, IP₃/DAG, PK-C Pathway is Triggered by Calmodulin

Brubaker-Purkey¹,

Woodruff²

2013

Journal of Insect Science

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In Drosophila melanogaster M. (Diptera: Drosophilidae), a phospholipase-C to proteininase-C signal cascade leads to the endocytic uptake of yolk precursor molecules. The data suggest that D. melanogaster has a phospholipase-C/proteinkinase-C signaling pathway similar to that previously shown to be required for vitellogenesis in the milkweed bug, Oncopeltus fasciatus Dallas (Hemiptera: Lygaeidae). Calmodulin, derived from epithelial cells and transported to the oocytes via gap junctions, may trigger this pathway. To investigate this, a series of known antagonists to various elements of the pathway were used. W-7 (which prevents calmodulin binding to phospholipase-C), U-73122 (which prevents activation of phospholipase-C), verapamil (which blocks Ca2+ release by IP3), HAG (which blocks diacylglycerol), and staurosporine (which inactivates proteinkinase-C) were each shown to inhibit endocytosis, thereby blocking formation of nascent yolk spheres.

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Section: Discussionmentioning

confidence: 99%

Vitellogenesis in the Fruit Fly,Drosophila melanogaster:Antagonists Demonstrate that the PLC, IP₃/DAG, PK-C Pathway is Triggered by Calmodulin

Brubaker-Purkey¹,

Woodruff²

2013

Journal of Insect Science

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“…Also, in insects, this communication channel has been confirmed to occur via gap junctions and the control molecule transported from follicle cells to oocytes has been identified as the 17 kDa protein calmodulin (Brooks & Woodruff, 2004). Moreover, Curran & Woodruff (2007) showed that CaM in its elongated shape was able to transit the vertebrate gap junctions between oocytes and the epithelial cells that surround them in the amphibian X. laevis and in fishes Danio rerio and Oryzias latipes (Curran & Woodruff, 2007).…”

Section: Discussionmentioning

confidence: 99%

Involvement of cAMP and calmodulin in endocytic yolk uptake duringXenopus laevisoogenesis

Luque

Serrano

Mónaco

et al. 2011

Zygote

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The aim of the present study was to show the participation and physiological role of calmodulin (CaM) and cAMP during vitellogenin endocytic uptake in the amphibian Xenopus laevis. The results showed a differential distribution of CaM in the ovary follicles during oogenesis. The CaM intracellular localization was not affected by gap junction's downregulation and CaM inhibition did not completely abolished the endocytic activity of oocytes. We showed that cAMP was able to completely rescue the endocytic competence in follicles in which gap junctional communication had been disrupted by octanol. Moreover cAMP was capable of restoring oocyte endocytic capability in the presence of octanol and stelazine, a CaM inhibitor. We propose that, in Vtg uptake regulation, cAMP is upstream of CaM during the endocytic signalling pathway.

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“…CaM has even been shown to be able to pass through a gap junction, possibly due to its elongated shape [10,11]. Cx43 has been shown to interact with CaM, and a specific binding site was recently [12] localised to the cytoplasmic loop, between residues 136-158.…”

Section: Introductionmentioning

confidence: 99%

Complex formation between calmodulin and a peptide from the intracellular loop of the gap junction protein connexin43: Molecular conformation and energetics of binding

Myllykoski

Kuczera

Kursula

2009

Biophysical Chemistry

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. Complex formation between calmodulin and a peptide from the intracellular loop of the gap junction protein connexin43: Molecular conformation and energetics of binding. Biophysical Chemistry, Elsevier, 2009, 144 (3) This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT AbstractGap junctions are formed by a family of transmembrane proteins, connexins.Connexin43 is a widely studied member of the family, being ubiquitously expressed in a variety of tissues and a target of a large number of disease mutations. The intracellular loop of connexin43 has been shown to include a calmodulin binding domain, but detailed 3-dimensional data on the structure of the complex are not available. In this study, we used a synthetic peptide from this domain to reveal the conformation of the calmodulin-peptide complex by small angle X-ray scattering.Upon peptide binding, calmodulin lost its dumbbell shape, adopting a more globular conformation. We also studied the energetics of the interaction using calorimetry and computational methods. All our data indicate that calmodulin binds to the peptide from cx43 in the classical 'collapsed' conformation.

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Passage of 17kDa calmodulin through gap junctions of three vertebrate species

Cited by 11 publications

References 55 publications

Vitellogenesis in the Fruit Fly,Drosophila melanogaster:Antagonists Demonstrate that the PLC, IP₃/DAG, PK-C Pathway is Triggered by Calmodulin

Vitellogenesis in the Fruit Fly,Drosophila melanogaster:Antagonists Demonstrate that the PLC, IP₃/DAG, PK-C Pathway is Triggered by Calmodulin

Involvement of cAMP and calmodulin in endocytic yolk uptake duringXenopus laevisoogenesis

Complex formation between calmodulin and a peptide from the intracellular loop of the gap junction protein connexin43: Molecular conformation and energetics of binding

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Passage of 17kDa calmodulin through gap junctions of three vertebrate species

Cited by 11 publications

References 55 publications

Vitellogenesis in the Fruit Fly,Drosophila melanogaster:Antagonists Demonstrate that the PLC, IP3/DAG, PK-C Pathway is Triggered by Calmodulin

Vitellogenesis in the Fruit Fly,Drosophila melanogaster:Antagonists Demonstrate that the PLC, IP3/DAG, PK-C Pathway is Triggered by Calmodulin

Involvement of cAMP and calmodulin in endocytic yolk uptake duringXenopus laevisoogenesis

Complex formation between calmodulin and a peptide from the intracellular loop of the gap junction protein connexin43: Molecular conformation and energetics of binding

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Resources

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Vitellogenesis in the Fruit Fly,Drosophila melanogaster:Antagonists Demonstrate that the PLC, IP₃/DAG, PK-C Pathway is Triggered by Calmodulin

Vitellogenesis in the Fruit Fly,Drosophila melanogaster:Antagonists Demonstrate that the PLC, IP₃/DAG, PK-C Pathway is Triggered by Calmodulin