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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-38477

Stein, D; Charatsi, I; Cho, Y S; Zhang, Z; Nguyen, J; Delotto, Ro; Luschnig, S; Moussian, B (2010). Localization and activation of the Drosophila protease Easter require the ER-resident Saposin-like rotein Seele. Current Biology, 20(21):1953-1958.

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Abstract

Drosophila embryonic dorsal-ventral polarity is generated by a series of serine protease processing events in the egg perivitelline space. Gastrulation Defective processes Snake, which then cleaves Easter, which then processes Spätzle into the activating ligand for the Toll receptor [1-3]. seele was identified in a screen for mutations that, when homozygous in ovarian germline clones, lead to the formation of progeny embryos with altered embryonic patterning; maternal loss of seele function leads to the production of moderately dorsalized embryos [4]. By combining constitutively active versions of Gastrulation Defective, Snake, Easter, and Spätzle with loss-of-function alleles of seele, we find that Seele activity is dispensable for Spätzle-mediated activation of Toll but is required for Easter, Snake, and Gastrulation Defective to exert their effects on dorsal-ventral patterning. Moreover, Seele function is required specifically for secretion of Easter from the developing embryo into the perivitelline space and for Easter processing. Seele protein resides in the endoplasmic reticulum of blastoderm embryos, suggesting a role in the trafficking of Easter to the perivitelline space, prerequisite to its processing and function. Easter transport to the perivitelline space represents a previously unappreciated control point in the signal transduction pathway that controls Drosophila embryonic dorsal-ventral polarity.

Item Type:Journal Article, refereed, original work
Communities & Collections:07 Faculty of Science > Institute of Molecular Life Sciences
DDC:570 Life sciences; biology
Language:English
Date:09 November 2010
Deposited On:09 Nov 2010 18:15
Last Modified:27 Nov 2013 19:12
Publisher:Elsevier
ISSN:0960-9822
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:10.1016/j.cub.2010.09.069
PubMed ID:20970335
Citations:Web of Science®. Times Cited: 3
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