Retromer Subunits VPS35A and VPS29 Mediate Prevacuolar
Compartment (PVC) Function in Arabidopsis

J 2013

Retromer Subunits VPS35A and VPS29 Mediate Prevacuolar Compartment (PVC) Function in Arabidopsis

NODZYNSKI, Tomasz; Mugurel I FERARU; Sibylle HIRSCH; Riet DE RYCKE; Claudiu NICULAES et. al.

Základní údaje

Originální název

Retromer Subunits VPS35A and VPS29 Mediate Prevacuolar Compartment (PVC) Function in Arabidopsis

Autoři

NODZYNSKI, Tomasz; Mugurel I FERARU; Sibylle HIRSCH; Riet DE RYCKE; Claudiu NICULAES; Wout BOERJAN; Jelle VAN LEENE; Geert DE JAEGER; Steffen VANNESTE a Jiří FRIML

Vydání

Molecular Plant, Oxford, Oxford University Press, 2013, 1674-2052

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

Genetika a molekulární biologie

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 6.605

Kód RIV

RIV/00216224:14740/13:00072087

Organizační jednotka

Středoevropský technologický institut

DOI

https://doi.org/10.1093/mp/sst044

UT WoS

000327541200010

Klíčová slova anglicky

retromer; VPS35; VPS29; prevacuolar compartment (PVC); vacuolar trafficking; Arabidopsis thaliana

Štítky

ok, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 13. 2. 2014 20:51, Olga Křížová

Anotace

V originále

Arabidopsis mutants defective in subunits of the retromer complex VPS35A and VPS29 show comparable defects in subcellular trafficking and ectopic intracellular accumulation of membrane proteins. These retromer components mediate together the function of the prevacuolar compartment (PVC) and trafficking to the lytic vacuole.Intracellular protein routing is mediated by vesicular transport which is tightly regulated in eukaryotes. The protein and lipid homeostasis depends on coordinated delivery of de novo synthesized or recycled cargoes to the plasma membrane by exocytosis and their subsequent removal by rerouting them for recycling or degradation. Here, we report the characterization of protein affected trafficking 3 (pat3) mutant that we identified by an epifluorescence-based forward genetic screen for mutants defective in subcellular distribution of Arabidopsis auxin transporter PIN1GFP. While pat3 displays largely normal plant morphology and development in nutrient-rich conditions, it shows strong ectopic intracellular accumulations of different plasma membrane cargoes in structures that resemble prevacuolar compartments (PVC) with an aberrant morphology. Genetic mapping revealed that pat3 is defective in vacuolar protein sorting 35A (VPS35A), a putative subunit of the retromer complex that mediates retrograde trafficking between the PVC and trans-Golgi network. Similarly, a mutant defective in another retromer subunit, vps29, shows comparable subcellular defects in PVC morphology and protein accumulation. Thus, our data provide evidence that the retromer components VPS35A and VPS29 are essential for normal PVC morphology and normal trafficking of plasma membrane proteins in plants. In addition, we show that, out of the three VPS35 retromer subunits present in Arabidopsis thaliana genome, the VPS35 homolog A plays a prevailing role in trafficking to the lytic vacuole, presenting another level of complexity in the retromer-dependent vacuolar sorting.

Návaznosti

ED1.1.00/02.0068, projekt VaV

Název: CEITEC - central european institute of technology

EE2.3.30.0009, projekt VaV

Název: Zaměstnáním čerstvých absolventů doktorského studia k vědecké excelenci

Přiložené soubory

Nodzynski_et_al_2013_Mol_Plant.pdf

Požádat o autorskou verzi souboru

Citovat

NODZYNSKI, Tomasz; Mugurel I FERARU; Sibylle HIRSCH; Riet DE RYCKE; Claudiu NICULAES; Wout BOERJAN; Jelle VAN LEENE; Geert DE JAEGER; Steffen VANNESTE a Jiří FRIML. Retromer Subunits VPS35A and VPS29 Mediate Prevacuolar Compartment (PVC) Function in Arabidopsis. Molecular Plant. Oxford: Oxford University Press, 2013, roč. 6, č. 6, s. 1849-1862. ISSN 1674-2052. Dostupné z: https://doi.org/10.1093/mp/sst044.

@article{1165389,
   author = {Nodzynski, Tomasz and Feraru, Mugurel I and Hirsch, Sibylle and De Rycke, Riet and Niculaes, Claudiu and Boerjan, Wout and Van Leene, Jelle and De Jaeger, Geert and Vanneste, Steffen and Friml, Jiří},
   article_location = {Oxford},
   article_number = {6},
   doi = {https://doi.org/10.1093/mp/sst044},
   keywords = {retromer; VPS35; VPS29; prevacuolar compartment (PVC); vacuolar trafficking; Arabidopsis thaliana},
   language = {eng},
   issn = {1674-2052},
   journal = {Molecular Plant},
   title = {Retromer Subunits VPS35A and VPS29 Mediate Prevacuolar Compartment (PVC) Function in Arabidopsis},
   volume = {6},
   year = {2013}
}

TY  - JOUR
ID  - 1165389
AU  - Nodzynski, Tomasz - Feraru, Mugurel I - Hirsch, Sibylle - De Rycke, Riet - Niculaes, Claudiu - Boerjan, Wout - Van Leene, Jelle - De Jaeger, Geert - Vanneste, Steffen - Friml, Jiří
PY  - 2013
TI  - Retromer Subunits VPS35A and VPS29 Mediate Prevacuolar Compartment (PVC) Function in Arabidopsis
JF  - Molecular Plant
VL  - 6
IS  - 6
SP  - 1849-1862
EP  - 1849-1862
PB  - Oxford University Press
SN  - 16742052
KW  - retromer
KW  - VPS35
KW  - VPS29
KW  - prevacuolar compartment (PVC)
KW  - vacuolar trafficking
KW  - Arabidopsis thaliana
N2  - Arabidopsis mutants defective in subunits of the retromer complex VPS35A and VPS29 show comparable defects in subcellular trafficking and ectopic intracellular accumulation of membrane proteins. These retromer components mediate together the function of the prevacuolar compartment (PVC) and trafficking to the lytic vacuole.Intracellular protein routing is mediated by vesicular transport which is tightly regulated in eukaryotes. The protein and lipid homeostasis depends on coordinated delivery of de novo synthesized or recycled cargoes to the plasma membrane by exocytosis and their subsequent removal by rerouting them for recycling or degradation. Here, we report the characterization of protein affected trafficking 3 (pat3) mutant that we identified by an epifluorescence-based forward genetic screen for mutants defective in subcellular distribution of Arabidopsis auxin transporter PIN1GFP. While pat3 displays largely normal plant morphology and development in nutrient-rich conditions, it shows strong ectopic intracellular accumulations of different plasma membrane cargoes in structures that resemble prevacuolar compartments (PVC) with an aberrant morphology. Genetic mapping revealed that pat3 is defective in vacuolar protein sorting 35A (VPS35A), a putative subunit of the retromer complex that mediates retrograde trafficking between the PVC and trans-Golgi network. Similarly, a mutant defective in another retromer subunit, vps29, shows comparable subcellular defects in PVC morphology and protein accumulation. Thus, our data provide evidence that the retromer components VPS35A and VPS29 are essential for normal PVC morphology and normal trafficking of plasma membrane proteins in plants. In addition, we show that, out of the three VPS35 retromer subunits present in Arabidopsis thaliana genome, the VPS35 homolog A plays a prevailing role in trafficking to the lytic vacuole, presenting another level of complexity in the retromer-dependent vacuolar sorting.
ER  -

NODZYNSKI, Tomasz; Mugurel I FERARU; Sibylle HIRSCH; Riet DE RYCKE; Claudiu NICULAES; Wout BOERJAN; Jelle VAN LEENE; Geert DE JAEGER; Steffen VANNESTE a Jiří FRIML. Retromer Subunits VPS35A and VPS29 Mediate Prevacuolar Compartment (PVC) Function in Arabidopsis. \textit{Molecular Plant}. Oxford: Oxford University Press, 2013, roč.~6, č.~6, s.~1849-1862. ISSN~1674-2052. Dostupné z: https://doi.org/10.1093/mp/sst044.

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