Cysteine Repeat Domains and Adjacent Sequences Determine Distinct Bone Morphogenetic Protein Modulatory Activities of the Drosophila Sog Protein

Yu, Kweon; Kang, Kyung‐Hwa; Heine, Petra; Pyati, Ujwal J.; Srinivasan, Shaila; Biehs, Brian; Kimelman, David; Bier, Ethan

doi:10.1534/genetics.166.3.1323

Cited by 25 publications

(34 citation statements)

References 50 publications

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“…BMP-2 preferentially binds to VWC1 and VWC3, and BMP-7 does so to VWC1 and VWC4. These results are consistent with the findings of genetic studies with Sog showing that VWC1 of Sog inhibited Dpp and VWC4 interfered selectively with Gbb (40). Therefore, the effect of adjacent non-VWC sequences on in vivo Sog activities seems not to be generated by their binding specificities for BMPs.…”

Section: Discussionsupporting

confidence: 90%

“…The so-called Supersog, consisting of VWC1 and part or complete segment between VWC1 and VWC2, blocked the effects of both Gbb and BMP-2/4 homologue Dpp. A combination of VWC1-segment-VWC2 promoted BMP activity (40). It seems that the VWC domains interact with adjacent non-VWC sequences to create forms of Sog with distinct BMP modulatory activities in vivo.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

von Willebrand Factor Type C Domain-containing Proteins Regulate Bone Morphogenetic Protein Signaling through Different Recognition Mechanisms

Zhang

Huang

Qiu

et al. 2007

Journal of Biological Chemistry

130

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Section: Discussionsupporting

confidence: 90%

Section: Discussionmentioning

confidence: 99%

von Willebrand Factor Type C Domain-containing Proteins Regulate Bone Morphogenetic Protein Signaling through Different Recognition Mechanisms

Zhang

Huang

Qiu

et al. 2007

Journal of Biological Chemistry

130

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“…This function of CRIM1 is mainly achieved by its interaction with BMPs via the CRR-containing portion of the protein. These CRRs are also found in the BMP antagonists, vertebrate chordin, and Drosophila sog and are responsible for the binding and regulation of BMPs (19)(20)(21)(22). However, until now, the function of the N-terminal IGF-binding protein motif of CRIM1 is still unknown.…”

Section: Discussionmentioning

confidence: 99%

Invertebrate Hematopoiesis: An Astakine-Dependent Novel Hematopoietic Factor

Lin

Söderhäll

2011

The Journal of Immunology

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A novel factor, named crustacean hematopoietic factor (CHF), was identified from a library of suppression subtractive hybridization with the aim to find downstream genes of an invertebrate cytokine, astakine 1, in the freshwater crayfish Pacifastacus leniusculus. CHF is a small cysteine-rich protein (∼9 kDa) with high similarity to the N-terminal region of vertebrate CRIM1 in containing an insulin growth factor binding protein variant motif with unknown function. CHF was found to be induced in primary cell cultures of crayfish hematopoietic tissue (Hpt) cells (precursors of crayfish blood cells) after treatment with astakine 1. Silencing of CHF did not affect the renewal of Hpt cells in vitro, but induced apoptosis of Hpt cells. CHF is exclusively expressed in the blood cell lineage of crayfish (Hpt cells and blood cells), and in vivo RNA interference experiments show that knockdown of this gene results in severe loss of blood cells and a higher apoptotic rate in Hpt. Our data further suggest that crayfish CHF is critical for the survival of hemocytes and Hpt cells by preventing their apoptosis, thus it plays an important role in hemocyte homeostasis in crayfish. Our study of CHF may also shed light on the function of this untypical insulin growth factor binding protein motif located in the N-terminal of vertebrate CRIM1.

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“…The UAS:Ppt1 transgenic lines were previously described in Korey and MacDonald (2003). All other lines used in this study were obtained from Bloomington except for the following: UAS:mys bPS (Beumer et al 1999), fasII eb112 (Grenningloh et al 1991), UAS:fasII (Holmes and Heilig 1999), faf BX4 , and UAS:faf (Huang et al 1995), endoA D4 and UAS:endoA (Verstreken et al 2003), UAS:dFos (Eresh et al 1997), UAS:sax (Yu et al 2004), UAS:syt1 (Littleton et al 1999), and UAS:stonedA and UAS:stonedB (Estes et al 2003).…”

Section: Methodsmentioning

confidence: 99%

Genetic Modifiers of Drosophila Palmitoyl–Protein Thioesterase 1-Induced Degeneration

Buff¹,

Smith²,

Korey

2007

Genetics

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Infantile neuronal ceroid lipofuscinosis (INCL) is a pediatric neurodegenerative disease caused by mutations in the human CLN1 gene. CLN1 encodes palmitoyl-protein thioesterase 1 (PPT1), suggesting an important role for the regulation of palmitoylation in normal neuronal function. To further elucidate Ppt1 function, we performed a gain-of-function modifier screen in Drosophila using a collection of enhancerpromoter transgenic lines to suppress or enhance the degeneration produced by overexpression of Ppt1 in the adult visual system. Modifier genes identified in our screen connect Ppt1 function to synaptic vesicle cycling, endo-lysosomal trafficking, synaptic development, and activity-dependent remodeling of the synapse. Furthermore, several homologs of the modifying genes are known to be regulated by palmitoylation in other systems and may be in vivo substrates for Ppt1. Our results complement recent work on mouse Ppt1À/À cells that shows a reduction in synaptic vesicle pools in primary neuronal cultures and defects in endosomal trafficking in human fibroblasts. The pathways and processes implicated by our modifier loci shed light on the normal cellular function of Ppt1. A greater understanding of Ppt1 function in these cellular processes will provide valuable insight into the molecular etiology of the neuronal dysfunction underlying the disease.

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Cysteine Repeat Domains and Adjacent Sequences Determine Distinct Bone Morphogenetic Protein Modulatory Activities of the Drosophila Sog Protein

Abstract: The Drosophila short gastrulation gene (sog) encodes a large extracellular protein (Sog) that inhibits signaling by BMP-related ligands.

Cited by 25 publications

References 50 publications

von Willebrand Factor Type C Domain-containing Proteins Regulate Bone Morphogenetic Protein Signaling through Different Recognition Mechanisms

von Willebrand Factor Type C Domain-containing Proteins Regulate Bone Morphogenetic Protein Signaling through Different Recognition Mechanisms

Invertebrate Hematopoiesis: An Astakine-Dependent Novel Hematopoietic Factor

Genetic Modifiers of Drosophila Palmitoyl–Protein Thioesterase 1-Induced Degeneration

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