Plant ESCRT protein ALIX coordinates with retromer complex in regulating receptor-mediated sorting of soluble vacuolar proteins.
Plant ESCRT protein ALIX coordinates with retromer complex in regulating receptor-mediated sorting of soluble vacuolar proteins.
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植物 ESCRT 蛋白 ALIX 与逆转录体复合物协调调节受体介导的可溶性液泡蛋白分选
DOI:
10.1073/pnas.2200492119
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发表时间:
2022-05-17
影响因子:
11.1
通讯作者:
中科院分区:
文献类型:
--
作者:
The endosomal sorting complex required for transport (ESCRT) machinery in multicellular organisms plays canonical functions in multivesicular body (MVB) biogenesis and membrane protein sorting. Nonetheless, its critical role in the sorting of soluble vacuolar proteins and its interplay with endosomal recycling machinery have yet to be reported. In this study, we demonstrate that Arabidopsis ESCRT-associated ALIXinteracts with the retromer core subunitsto regulate their recruitment onto endosome membrane for recycling of vacuolar sorting receptors (VSRs) for efficient sorting of soluble vacuolar proteins. This work provides molecular insights into the unique properties of ALIX in regulating vacuolar transport of soluble proteins, thus shedding new light on the crosstalk and coordination between the vacuolar trafficking and endosomal recycling pathways in plants. Vacuolar proteins play essential roles in plant physiology and development, but the factors and the machinery regulating their vesicle trafficking through the endomembrane compartments remain largely unknown. We and others have recently identified an evolutionarily conserved plant endosomal sorting complex required for transport (ESCRT)-associated protein apoptosis-linked gene-2 interacting protein X (ALIX), which plays canonical functions in the biogenesis of the multivesicular body/prevacuolar compartment (MVB/PVC) and in the sorting of ubiquitinated membrane proteins. In this study, we elucidate the roles and underlying mechanism of ALIX in regulating vacuolar transport of soluble proteins, beyond its conventional ESCRT function in eukaryotic cells. We show that ALIX colocalizes and physically interacts with the retromer core subunits Vps26 and Vps29 in planta. Moreover, double-mutant analysis reveals the genetic interaction of ALIX with Vps26 and Vps29 for regulating trafficking of soluble vacuolar proteins. Interestingly, depletion of ALIX perturbs membrane recruitment of Vps26 and Vps29 and alters the endosomal localization of vacuolar sorting receptors (VSRs). Taken together, ALIX functions as a unique retromer core subcomplex regulator by orchestrating receptor-mediated vacuolar sorting of soluble proteins.
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DOI:
10.1016/j.str.2009.04.007
发表时间:
2009-06-10
期刊:
Structure (London, England : 1993)
影响因子:
--
作者:
Pires R;Hartlieb B;Signor L;Schoehn G;Lata S;Roessle M;Moriscot C;Popov S;Hinz A;Jamin M;Boyer V;Sadoul R;Forest E;Svergun DI;Göttlinger HG;Weissenhorn W
通讯作者:
Weissenhorn W
影响因子:
6.9
作者:
Wang J;Tse YC;Hinz G;Robinson DG;Jiang L
通讯作者:
Jiang L
影响因子:
11.6
作者:
Humair, D;Felipe, DH;Paris, N
通讯作者:
Paris, N
影响因子:
7.4
作者:
Kolb, Cornelia;Nagel, Marie-Kristin;Isono, Erika
通讯作者:
Isono, Erika
影响因子:
64.8
作者:
Jaillais, Yvon;Fobis-Loisy, Isabelle;Gaude, Thierry
通讯作者:
Gaude, Thierry