The M3 Phosphorylation Site Is Required for Trafficking and Biological Roles of PIN-FORMED1, 2, and 7 in Arabidopsis.
The M3 Phosphorylation Site Is Required for Trafficking and Biological Roles of PIN-FORMED1, 2, and 7 in Arabidopsis.
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DOI：
10.3389/fpls.2016.01479
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发表时间：
2016
影响因子：
5.6
通讯作者：
Cho HT
中科院分区：
文献类型：
--
作者：
Ki D;Sasayama D;Cho HT
不对称定位的PIN- formed （PIN）生长素外排载体在调节生长素定向胞间运动、产生局部生长素梯度以及多种生长素介导的生长发育中起着关键作用。pin的极性定位是由pin的中心亲水环（HL）磷酸化控制的。尽管M3磷酸化位点，包括可磷酸化的5个Ser/Thr残基，在长HL-PINs中是保守的，但其天然作用仅在PIN3中被表征。在这项研究中，我们检测了PIN1、PIN2和PIN7的M3磷酸化位点在这些pin在其天然表达组织中的细胞内运输、磷酸化和生物学功能中的作用。PIN1- hl M3位点磷酸化残基的磷酸化缺陷突变导致PIN1亚细胞极性改变，并导致PIN1介导的生物学功能缺陷，如子叶发育、营养叶分叶和生殖器官发育。PIN7的M3突变干扰了其在根小柱细胞中响应重力刺激的极性循环，部分破坏了根的向地性。另一方面，PIN2的M3位点被证明是其靶向质膜所必需的。体外磷酸化实验表明，PIN1的M3磷酸化残基是PINOID激酶的部分靶点。我们的数据表明，M3磷酸化位点在长hl - pin中是功能性保守的，它在hl - pin的亚细胞运输和生长素介导的发育过程中发挥作用。
Asymmetrically localized PIN-FORMED (PIN) auxin efflux carriers play key roles in regulating directional intercellular auxin movement, generating local auxin gradients, and diverse auxin-mediated growth and development. The polar localization of PINs is controlled by phosphorylation in the central hydrophilic loop (HL) of PINs. Although the M3 phosphorylation site, including phosphorylatable 5 Ser/Thr residues, is conserved among long HL-PINs, its native role has only been characterized in PIN3. In this study, we examined the role of M3 phosphorylation site of PIN1, PIN2, and PIN7 in intracellular trafficking, phosphorylation, and biological functions of those PINs in their native expressing tissues. Phosphorylation-defective mutations of the phosphorylatable residues in the M3 site of PIN1-HL led to alteration in subcellular polarity of PIN1 and caused defects in PIN1-mediated biological functions such as cotyledon development, phyllotaxy of vegetative leaves, and development of reproductive organs. The M3 mutations of PIN7 interfered with its polar recycling in the root columella cell in response to gravity stimulus and partially disrupted root gravitropism. On the other hand, the M3 site of PIN2 was shown to be necessary for its targeting to the plasma membrane. In vitro phosphorylation assay showed that the M3 phosphorylation residues of PIN1 are the partial targets by PINOID kinase. Our data suggest that the M3 phosphorylation site is functionally conserved among long HL-PINs by playing roles for their subcellular trafficking and auxin-mediated developmental processes.
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影响因子：
64.8
作者：
Blilou, I;Xu, J;Scheres, B
通讯作者：
Scheres, B
M3磷酸化基序在拟南芥根部毛细胞中的细胞内运输在功能上保守了。
影响因子：
5.3
作者：
Sasayama D;Ganguly A;Park M;Cho HT
通讯作者：
Cho HT
影响因子：
11.6
作者：
Ganguly, Anindya;Park, Minho;Cho, Hyung-Taeg
通讯作者：
Cho, Hyung-Taeg
影响因子：
64.8
作者：
Dhonukshe, Pankaj;Tanaka, Hirokazu;Goh, Tatsuaki;Ebine, Kazuo;Mahonen, Ari Pekka;Prasad, Kalika;Blilou, Ikram;Geldner, Niko;Xu, Jian;Uemura, Tomohiro;Chory, Joanne;Ueda, Takashi;Nakano, Akihiko;Scheres, Ben;Friml, Jiri
通讯作者：
Friml, Jiri
影响因子：
12.3
作者：
Krecek P;Skupa P;Libus J;Naramoto S;Tejos R;Friml J;Zazímalová E
通讯作者：
Zazímalová E