Cytokinin inhibits cotton fiber initiation by disrupting PIN3a-mediated asymmetric accumulation of auxin in the ovule epidermis

Cytokinin inhibits cotton fiber initiation by disrupting PIN3a-mediated asymmetric accumulation of auxin in the ovule epidermis
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细胞分裂素通过破坏 PIN3a 介导的胚珠表皮中生长素的不对称积累来抑制棉纤维的起始

DOI:
10.1093/jxb/erz162
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发表时间:
2019-04
影响因子:
6.9
通讯作者:
Pei Yan
Pei Yan
中科院分区:
生物学1区
文献类型:
--
作者:
Zeng Jianyan;Zhang Mi;Hou Lei;Bai Wenqin;Yan Xingying;Hou Nan;Wang Hongxing;Huang Juan;Zhao Juan;Pei Yan

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摘要生长素依赖的细胞扩增是棉花纤维细胞发生的关键,而纤维细胞的发生又决定着棉花纤维的产量和品质。然而,对这一过程的监管还远未得到很好的理解。在这项研究中,我们证明了细胞分裂素(CK)和生长素之间的拮抗作用对棉花纤维的起始。离体和植物试验表明,CK水平的提高可以减少胚珠珠被中生长素的积累,这可能是无纤维突变体xu142fl缺陷的原因。反过来,补充生长素可以恢复CK处理的胚珠和突变胚珠的纤维生长。我们进一步发现,GhPIN 3a是一个关键的生长素转运纤维细胞的启动和极性定位到非纤维细胞的质膜,但不是那些纤维细胞。这种极性定位允许生长素在胚珠珠被内运输,同时特异性地在纤维细胞中积累。我们发现,CKs拮抗促进作用的生长素纤维细胞起始破坏不对称积累的生长素在胚珠表皮通过下调GhPIN3a和干扰的极性定位的蛋白质。
Abstract Auxin-dependent cell expansion is crucial for initiation of fiber cells in cotton (Gossypium hirsutum), which ultimately determines fiber yield and quality. However, the regulation of this process is far from being well understood. In this study, we demonstrate an antagonistic effect between cytokinin (CK) and auxin on cotton fiber initiation. In vitro and in planta experiments indicate that enhanced CK levels can reduce auxin accumulation in the ovule integument, which may account for the defects in the fiberless mutant xu142fl. In turn, supplementation with auxin can recover fiber growth of CK-treated ovules and mutant ovules. We further found that GhPIN3a is a key auxin transporter for fiber-cell initiation and is polarly localized to the plasma membranes of non-fiber cells, but not to those of fiber cells. This polar localization allows auxin to be transported within the ovule integument while specifically accumulating in fiber cells. We show that CKs antagonize the promotive effect of auxin on fiber cell initiation by undermining asymmetric accumulation of auxin in the ovule epidermis through down-regulation of GhPIN3a and disturbance of the polar localization of the protein.
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