The Shot CH1 domain recognises a distinct form of F-actin during Drosophila oocyte determination

The Shot CH1 domain recognises a distinct form of F-actin during Drosophila oocyte determination
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Shot CH1 结构域在果蝇卵母细胞测定过程中识别不同形式的 F-肌动蛋白

DOI:
10.1101/2023.01.18.524359
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发表时间:
2023
期刊:
--
影响因子:
--
通讯作者:
Nashchekin D
Nashchekin D
中科院分区:
--
文献类型:
--
作者:
Nashchekin D

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在果蝇中,多细胞雌性生殖系包囊中只有一个细胞被指定为卵母细胞,哺乳动物也有类似的过程。卵母细胞选择的破囊线索是由融合体提供的,融合体是一种连接包囊中所有细胞的管状结构。果蝇spectraplakin射击定位于融合体,并将其不对称性转化为一个极化的微管网络,这对卵母细胞的特化至关重要,但射击如何识别融合体尚不清楚。在这里,我们证明,肌动蛋白结合域(ABD)的拍摄是必要的,足以本地化拍摄的融合体和介导的拍摄功能,在卵母细胞规格与微管结合域。Shot ABD的钙调蛋白同源结构域1识别梭体F-肌动蛋白,并需要钙调蛋白同源结构域2将其与囊肿中其他形式的F-肌动蛋白区分开来。相比之下,utrophin、Fimelatin、Filamin、Lifeact和F-tractin的ABD不识别融合体F-actin。因此,我们建议,拍摄传播融合体不对称性,通过识别一个特定的构象状态的F-肌动蛋白的融合体。
In Drosophila, only one cell in a multicellular female germline cyst is specified as an oocyte and a similar process occurs in mammals. The symmetry-breaking cue for oocyte selection is provided by the fusome, a tubular structure connecting all cells in the cyst. The Drosophila spectraplakin Shot localises to the fusome and translates its asymmetry into a polarised microtubule network that is essential for oocyte specification, but how Shot recognises the fusome is unclear. Here, we demonstrate that the actin-binding domain (ABD) of Shot is necessary and sufficient to localise Shot to the fusome and mediates Shot function in oocyte specification together with the microtubule-binding domains. The calponin homology domain 1 of the Shot ABD recognises fusomal F-actin and requires calponin homology domain 2 to distinguish it from other forms of F-actin in the cyst. By contrast, the ABDs of utrophin, Fimbrin, Filamin, Lifeact and F-tractin do not recognise fusomal F-actin. We therefore propose that Shot propagates fusome asymmetry by recognising a specific conformational state of F-actin on the fusome.
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影响因子: 10.5
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发表时间: 2004-01-20
期刊: CURRENT BIOLOGY
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