Gastrulation Defective is a serine protease involved in activating the receptor Toll to polarize the
            <i>Drosophila</i>
            embryo

Han, Jie; Lee, Si Hyoung; Tan, Yue-Qing; LeMosy, Ellen K.; Hashimoto, Carl

doi:10.1073/pnas.97.16.9093

Cited by 30 publications

(35 citation statements)

References 32 publications

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“…That depiction strongly resembled a Drosophila melanogaster protease called gastrulation defective (GD), which is a 72-kD extracellular Ser protease involved in a protease cascade leading to dorsal-ventral signaling (Konrad et al, 1998;Han et al, 2000;DeLotto, 2001;Dissing et al, 2001;LeMosy et al, 2001). After purification and partial sequencing, it became clear that GD and SAS-1 and SAS-2 are structurally unrelated, although they may share some similar biological characteristics.…”

Section: Heparin and Autoproteolysismentioning

confidence: 99%

Purification and Characterization of Serine Proteases That Exhibit Caspase-Like Activity and Are Associated with Programmed Cell Death in Avena sativa

2004

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Victoria blight of Avena sativa (oat) is caused by the fungus Cochliobolus victoriae, which is pathogenic because of the production of the toxin victorin. The victorin-induced response in sensitive A. sativa has been characterized as a form of programmed cell death (PCD) and displays morphological and biochemical features similar to apoptosis, including chromatin condensation, DNA laddering, cell shrinkage, altered mitochondrial function, and ordered, substrate-specific proteolytic events. Victorin-induced proteolysis of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is shown to be prevented by caspase-specific and general protease inhibitors. Evidence is presented for a signaling cascade leading to Rubisco proteolysis that involves multiple proteases. Furthermore, two proteases that are apparently involved in the Rubisco proteolytic cascade were purified and characterized. These proteases exhibit caspase specificity and display amino acid sequences homologous to plant subtilisin-like Ser proteases. The proteases are constitutively present in an active form and are relocalized to the extracellular fluid after induction of PCD by either victorin or heat shock. The role of the enzymes as processive proteases involved in a signal cascade during the PCD response is discussed.

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Section: Heparin and Autoproteolysismentioning

confidence: 99%

Purification and Characterization of Serine Proteases That Exhibit Caspase-Like Activity and Are Associated with Programmed Cell Death in Avena sativa

2004

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“…Because our previous studies had suggested that GD activity depends on proteolytic processing, we initially tested the activities of two truncated GD forms. GD⌬N1 lacks amino acids 1 through 211 after signal sequence cleavage, where Lys-211 is the nearest basic residue N-terminal to the conserved catalytic domain and thus might serve as a cleavage site for GD activation (6,13). GD⌬N2 lacks amino acids 1 through 253, corresponding to a potential cleavage site suggested by Konrad et al (13) at the beginning of the conserved catalytic-domain sequence.…”

Section: Gd Triggers a Proteolytic Cascade By Activating Snake That Imentioning

confidence: 99%

“…Our recent studies have suggested that GD, the next downstream protease from Nudel, plays a more clearly instructive role in triggering the Toll signaling pathway (6). Unusual structural features of GD have made it uncertain whether this protein functions as a protease (13).…”

mentioning

confidence: 99%

Activation of a protease cascade involved in patterning the Drosophila embryo

LeMosy

Tan

Hashimoto

2001

Proc. Natl. Acad. Sci. U.S.A.

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101

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Dorsoventral patterning of the Drosophila embryo is initiated by a ventralizing signal. Production of this signal requires the serine proteases Gastrulation Defective (GD), Snake, and Easter, which genetic studies suggest act sequentially in a cascade that is activated locally in response to a ventral cue provided by the pipe gene. Here, we demonstrate biochemically that GD activates Snake, which in turn activates Easter. We also provide evidence that GD zymogen cleavage is important for triggering this cascade but is not spatially localized by pipe. Our results suggest that a broadly, rather than locally, activated protease cascade produces the ventralizing signal, so a distinct downstream step in this cascade must be spatially regulated to restrict signaling to the ventral side of the embryo.serine protease ͉ dorsoventral axis ͉ transfection

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“…4D). Members of group 1 are predicted to have one helix between Cys 3 and Cys 4 and one helix centered on a cysteine of the linker. A detailed analysis of group 1 reveals four subgroups depending on the number of cysteines in the linker (1a-1d).…”

Section: -Loop Prevents Access To the Activation Site-mentioning

confidence: 99%

Structure-Function Analysis of Grass Clip Serine Protease Involved in Drosophila Toll Pathway Activation

Kellenberger

Leone

Coquet

et al. 2011

Journal of Biological Chemistry

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Gastrulation Defective is a serine protease involved in activating the receptor Toll to polarize the Drosophila embryo

Cited by 30 publications

References 32 publications

Purification and Characterization of Serine Proteases That Exhibit Caspase-Like Activity and Are Associated with Programmed Cell Death in Avena sativa

Purification and Characterization of Serine Proteases That Exhibit Caspase-Like Activity and Are Associated with Programmed Cell Death in Avena sativa

Activation of a protease cascade involved in patterning the Drosophila embryo

Structure-Function Analysis of Grass Clip Serine Protease Involved in Drosophila Toll Pathway Activation

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