N-linked glycosylation of AtVSR1 is important for vacuolar protein sorting in Arabidopsis.
N-linked glycosylation of AtVSR1 is important for vacuolar protein sorting in Arabidopsis.
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DOI：
10.1111/tpj.12696
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发表时间：
2014-12
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影响因子：
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通讯作者：
Jinbo Shen;Yu Ding;Caiji Gao;E. Rojo;Liwen Jiang
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文献类型：
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作者：
Jinbo Shen;Yu Ding;Caiji Gao;E. Rojo;Liwen Jiang
拟南芥液泡分选受体介导可溶性蛋白在分泌途径中向液泡分选。这些VSRs在翻译后通过附着n -聚糖进行修饰，但这种修饰的功能意义尚不清楚。本文研究了糖基化在拟南芥原生质体中AtVSR1的稳定性、转运和空泡蛋白转运中的作用。AtVSR1含有3个络合物型n -聚糖，分别位于n端“PA结构域”、中心区域和c端表皮生长因子重复结构域。我们已经证明：(i) n -聚糖不影响AtVSR1对空泡前室（PVCs）的靶向及其空泡降解；（ii） n -糖基化改变AtVSR1与货物蛋白的结合亲和力，影响货物进入液泡的运输。因此，AtVSR1的n -糖基化在其作为植物VSR的功能中起着至关重要的作用。
Vacuolar sorting receptors (VSRs) in Arabidopsis mediate the sorting of soluble proteins to vacuoles in the secretory pathway. The VSRs are post-translationally modified by the attachment of N-glycans, but the functional significance of such a modification remains unknown. Here we have studied the role(s) of glycosylation in the stability, trafficking and vacuolar protein transport of AtVSR1 in Arabidopsis protoplasts. AtVSR1 harbors three complex-type N-glycans, which are located in the N-terminal 'PA domain', the central region and the C-terminal epidermal growth factor repeat domain, respectively. We have demonstrated that: (i) the N-glycans do not affect the targeting of AtVSR1 to pre-vacuolar compartments (PVCs) and its vacuolar degradation; and (ii) N-glycosylation alters the binding affinity of AtVSR1 to cargo proteins and affects the transport of cargo into the vacuole. Hence, N-glycosylation of AtVSR1 plays a critical role in its function as a VSR in plants.