STRICA, a novel Drosophila melanogaster caspase with an unusual serine/threonine-rich prodomain, interacts with DIAP1 and DIAP2
STRICA, a novel Drosophila melanogaster caspase with an unusual serine/threonine-rich prodomain, interacts with DIAP1 and DIAP2
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DOI：
10.1038/sj.cdd.4400864
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发表时间：
2001-04-01
影响因子：
12.4
通讯作者：
Kumar, S
中科院分区：
文献类型：
--
作者：
Doumanis, J;Quinn, L;Kumar, S
最近发表的黑腹果蝇基因组序列预测苍蝇中有七个半胱天冬酶。其中五种半胱天冬酶以前已经被表征，在这里，我们描述了果蝇半胱天冬酶，STRICA，STRICA是一种具有长氨基末端前结构域的半胱天冬酶，其缺乏任何半胱天冬酶募集结构域或死亡效应结构域。相反，STRICA的前结构域由独特的丝氨酸/苏氨酸片段组成。在胚胎、幼虫、脓疱和成年动物中检测到低水平的strica表达。STRICA是一种细胞质蛋白，其在过表达时引起培养的果蝇SL 2细胞中的凋亡，所述细胞被DIAP 1部分抑制。有趣的是，与其他苍蝇半胱天冬酶不同，在共转染实验中，STRICA显示出与DIAP 2的物理关联。这些结果表明，STRICA可能具有独特的细胞功能。
The recently published genome sequence of Drosophila melanogaster predicts seven caspases in the fly. Five of these caspases have been previously characterised, Here, we describe the Drosophila caspase, STRICA, STRICA is a caspase with a long amino-terminal prodomain that lacks any caspase recruitment domain or death effector domain. Instead, the prodomain of STRICA consists of unique serine/ threonine stretches. Low levels of strica expression were detected in embryos, larvae, pupae and adult animals. STRICA is a cytoplasmic protein that, upon overexpression, caused apoptosis in cultured Drosophila SL2 cells that was partially suppressed by DIAP1, Interestingly, unlike other fly caspases, STRICA showed physical association with DIAP2, in cotransfection experiments. These results suggest that STRICA may have a unique cellular function.