The PS2 integrin ligand tiggrin is required for proper muscle function in Drosophila.
The PS2 integrin ligand tiggrin is required for proper muscle function in Drosophila.
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发表时间：
1998-05
期刊：
影响因子：
4.6
通讯作者：
T. Bunch;M. Graner;L. Fessler;J. Fessler;K. D. Schneider;A. Kerschen;L. P. Choy;B. Burgess;D. Brower
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作者：
T. Bunch;M. Graner;L. Fessler;J. Fessler;K. D. Schneider;A. Kerschen;L. P. Choy;B. Burgess;D. Brower
Tiggrin是一种新的果蝇PS2整合素的细胞外基质配体。我们已经使用了侧翼P元素来生成一个精确的tiggrin缺失。大多数缺乏老虎精蛋白的苍蝇都会以幼虫或蛹的形式死亡。少数成虫确实出现了，这些看起来相对正常，只显示出畸形的腹部和低频率的翅膀缺陷。对幼虫的检查表明，突变体的肌肉连接、功能和形态都有缺陷。在虎纹突变体中，延长幼虫长度的肌肉收缩波要慢得多。对体壁肌肉的直接检查显示，肌肉附着部位存在缺陷，在那里，tiggrin被特别定位，肌肉看起来更薄。表达tiggrin的转基因能够挽救突变型Tigggrin。表达突变型Tigggrin的转基因细胞，其Arg-Gly-Asp(RGD)整合素识别序列已突变为Leu-Gly-Ala(LGA)，其拯救能力大大降低，但显著。细胞铺展实验未检测到该突变的tiggrin与PS2整合素的相互作用。因此，虽然RGD序列对PS2的相互作用和整个果蝇的全部活动是关键的，但突变的tiggrin保留了一些功能(S)，这些功能可能是通过与其他细胞外基质分子或细胞表面受体的相互作用来调节的
Tiggrin is a novel extracellular matrix ligand for the Drosophila PS2 integrins. We have used flanking P elements to generate a precise deletion of tiggrin. Most flies lacking tiggrin die as larvae or pupae. A few adults do emerge and these appear to be relatively normal, displaying only misshapen abdomens and a low frequency of wing defects. Examination of larvae shows that muscle connections, function and morphology are defective in tiggrin mutants. Muscle contraction waves that extend the length of the larvae are much slower in tiggrin mutants. Direct examination of bodywall muscles shows defects in muscle attachment sites, where tiggrin is specifically localized, and muscles appear thinner. Transgenes expressing tiggrin are capable of rescuing tiggrin mutant phenotypes. Transgenes expressing a mutant tiggrin, whose Arg-Gly-Asp (RGD) integrin recognition sequence has been mutated to Leu-Gly-Ala (LGA) show much reduced, but significant, rescuing ability. Cell spreading assays detect no interactions of this mutant tiggrin with PS2 integrins. Therefore, while the RGD sequence is critical for PS2 interactions and full activity in the whole fly, the mutant tiggrin retains some function(s) that are probably mediated by interactions with other ECM molecules or cell surface receptors