Publication

Saccharomyces cerevisiae cells lacking Pex3 contain membrane vesicles that harbor a subset of peroxisomal membrane proteins

Wroblewska, J. P., Cruz-Zaragoza, L. D., Yuan, W., Schummer, A., Chuartzman, S. G., de Boer, R., Oeljeklaus, S., Schuldiner, M., Zalckvar, E., Warscheid, B., Erdmann, R. & van der Klei, I. J., Oct-2017, In : Biochimica et Biophysica Acta - Molecular Cell Research. 1864, 10, p. 1656-1667 12 p., bbamcr.2017.05.021.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Wroblewska, J. P., Cruz-Zaragoza, L. D., Yuan, W., Schummer, A., Chuartzman, S. G., de Boer, R., ... van der Klei, I. J. (2017). Saccharomyces cerevisiae cells lacking Pex3 contain membrane vesicles that harbor a subset of peroxisomal membrane proteins. Biochimica et Biophysica Acta - Molecular Cell Research, 1864(10), 1656-1667. [bbamcr.2017.05.021]. https://doi.org/10.1016/j.bbamcr.2017.05.021

Author

Wroblewska, Justyna P. ; Cruz-Zaragoza, Luis Daniel ; Yuan, Wei ; Schummer, Andreas ; Chuartzman, Silvia G. ; de Boer, Rinse ; Oeljeklaus, Silke ; Schuldiner, Maya ; Zalckvar, Einat ; Warscheid, Bettina ; Erdmann, Ralf ; van der Klei, Ida J. / Saccharomyces cerevisiae cells lacking Pex3 contain membrane vesicles that harbor a subset of peroxisomal membrane proteins. In: Biochimica et Biophysica Acta - Molecular Cell Research. 2017 ; Vol. 1864, No. 10. pp. 1656-1667.

Harvard

Wroblewska, JP, Cruz-Zaragoza, LD, Yuan, W, Schummer, A, Chuartzman, SG, de Boer, R, Oeljeklaus, S, Schuldiner, M, Zalckvar, E, Warscheid, B, Erdmann, R & van der Klei, IJ 2017, 'Saccharomyces cerevisiae cells lacking Pex3 contain membrane vesicles that harbor a subset of peroxisomal membrane proteins', Biochimica et Biophysica Acta - Molecular Cell Research, vol. 1864, no. 10, bbamcr.2017.05.021, pp. 1656-1667. https://doi.org/10.1016/j.bbamcr.2017.05.021

Standard

Saccharomyces cerevisiae cells lacking Pex3 contain membrane vesicles that harbor a subset of peroxisomal membrane proteins. / Wroblewska, Justyna P.; Cruz-Zaragoza, Luis Daniel; Yuan, Wei; Schummer, Andreas; Chuartzman, Silvia G.; de Boer, Rinse; Oeljeklaus, Silke; Schuldiner, Maya; Zalckvar, Einat; Warscheid, Bettina; Erdmann, Ralf; van der Klei, Ida J.

In: Biochimica et Biophysica Acta - Molecular Cell Research, Vol. 1864, No. 10, bbamcr.2017.05.021, 10.2017, p. 1656-1667.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Wroblewska JP, Cruz-Zaragoza LD, Yuan W, Schummer A, Chuartzman SG, de Boer R et al. Saccharomyces cerevisiae cells lacking Pex3 contain membrane vesicles that harbor a subset of peroxisomal membrane proteins. Biochimica et Biophysica Acta - Molecular Cell Research. 2017 Oct;1864(10):1656-1667. bbamcr.2017.05.021. https://doi.org/10.1016/j.bbamcr.2017.05.021


BibTeX

@article{a3a3f35dac474858936ca3f29146cd85,
title = "Saccharomyces cerevisiae cells lacking Pex3 contain membrane vesicles that harbor a subset of peroxisomal membrane proteins",
abstract = "Pex3 has been proposed to be important for the exit of peroxisomal membrane proteins (PMPs) from the ER, based on the observation that PMPs accumulate at the ER in Saccharomyces cerevisiae pex3 mutant cells.Using a combination of microscopy and biochemical approaches, we show that a subset of the PMPs, including the receptor docking protein Pex14, localizes to membrane vesicles in S. cerevisiae pex3 cells. These vesicles are morphologically distinct from the ER and do not co-sediment with ER markers in cell fractionation experiments. At the vesicles, Pex14 assembles with other peroxins (Pex13, Pex17, and Pex5) to form a complex with a composition similar to the PTS1 import pore in wild-type cells.Fluorescence microscopy studies revealed that also the PTS2 receptor Pex7, the importomer organizing peroxin Pex8, the ubiquitin conjugating enzyme Pex4 with its recruiting PMP Pex22, as well as Pex15 and Pex25 co-localize with Pex14. Other peroxins (including the RING finger complex and Pex27) did not accumulate at these structures, of which Pexll localized to mitochondria. In line with these observations, proteomic analysis showed that in addition to the docking proteins and Pex5, also Pex7, Pex4/Pex22 and Pex25 were present in Pex14 complexes isolated from pex3 cells. However, formation of the entire importomer was not observed, most likely because Pex8 and the RING proteins were absent in the Pex14 protein complexes.Our data suggest that peroxisomal membrane vesicles can form in the absence of Pex3 and that several PMPs can insert in these vesicles in a Pex3 independent manner.",
keywords = "peroxisome, organelle, Pex3, peroxisomal membrane protein, protein sorting, endoplasmatic reticulum, yeast, Saccharomyces cerevisiae",
author = "Wroblewska, {Justyna P.} and Cruz-Zaragoza, {Luis Daniel} and Wei Yuan and Andreas Schummer and Chuartzman, {Silvia G.} and {de Boer}, Rinse and Silke Oeljeklaus and Maya Schuldiner and Einat Zalckvar and Bettina Warscheid and Ralf Erdmann and {van der Klei}, {Ida J.}",
note = "Copyright {\circledC} 2017. Published by Elsevier B.V.",
year = "2017",
month = "10",
doi = "10.1016/j.bbamcr.2017.05.021",
language = "English",
volume = "1864",
pages = "1656--1667",
journal = "Biochimica et Biophysica Acta - Molecular Cell Research",
issn = "0167-4889",
publisher = "ELSEVIER SCIENCE BV",
number = "10",

}

RIS

TY - JOUR

T1 - Saccharomyces cerevisiae cells lacking Pex3 contain membrane vesicles that harbor a subset of peroxisomal membrane proteins

AU - Wroblewska, Justyna P.

AU - Cruz-Zaragoza, Luis Daniel

AU - Yuan, Wei

AU - Schummer, Andreas

AU - Chuartzman, Silvia G.

AU - de Boer, Rinse

AU - Oeljeklaus, Silke

AU - Schuldiner, Maya

AU - Zalckvar, Einat

AU - Warscheid, Bettina

AU - Erdmann, Ralf

AU - van der Klei, Ida J.

N1 - Copyright © 2017. Published by Elsevier B.V.

PY - 2017/10

Y1 - 2017/10

N2 - Pex3 has been proposed to be important for the exit of peroxisomal membrane proteins (PMPs) from the ER, based on the observation that PMPs accumulate at the ER in Saccharomyces cerevisiae pex3 mutant cells.Using a combination of microscopy and biochemical approaches, we show that a subset of the PMPs, including the receptor docking protein Pex14, localizes to membrane vesicles in S. cerevisiae pex3 cells. These vesicles are morphologically distinct from the ER and do not co-sediment with ER markers in cell fractionation experiments. At the vesicles, Pex14 assembles with other peroxins (Pex13, Pex17, and Pex5) to form a complex with a composition similar to the PTS1 import pore in wild-type cells.Fluorescence microscopy studies revealed that also the PTS2 receptor Pex7, the importomer organizing peroxin Pex8, the ubiquitin conjugating enzyme Pex4 with its recruiting PMP Pex22, as well as Pex15 and Pex25 co-localize with Pex14. Other peroxins (including the RING finger complex and Pex27) did not accumulate at these structures, of which Pexll localized to mitochondria. In line with these observations, proteomic analysis showed that in addition to the docking proteins and Pex5, also Pex7, Pex4/Pex22 and Pex25 were present in Pex14 complexes isolated from pex3 cells. However, formation of the entire importomer was not observed, most likely because Pex8 and the RING proteins were absent in the Pex14 protein complexes.Our data suggest that peroxisomal membrane vesicles can form in the absence of Pex3 and that several PMPs can insert in these vesicles in a Pex3 independent manner.

AB - Pex3 has been proposed to be important for the exit of peroxisomal membrane proteins (PMPs) from the ER, based on the observation that PMPs accumulate at the ER in Saccharomyces cerevisiae pex3 mutant cells.Using a combination of microscopy and biochemical approaches, we show that a subset of the PMPs, including the receptor docking protein Pex14, localizes to membrane vesicles in S. cerevisiae pex3 cells. These vesicles are morphologically distinct from the ER and do not co-sediment with ER markers in cell fractionation experiments. At the vesicles, Pex14 assembles with other peroxins (Pex13, Pex17, and Pex5) to form a complex with a composition similar to the PTS1 import pore in wild-type cells.Fluorescence microscopy studies revealed that also the PTS2 receptor Pex7, the importomer organizing peroxin Pex8, the ubiquitin conjugating enzyme Pex4 with its recruiting PMP Pex22, as well as Pex15 and Pex25 co-localize with Pex14. Other peroxins (including the RING finger complex and Pex27) did not accumulate at these structures, of which Pexll localized to mitochondria. In line with these observations, proteomic analysis showed that in addition to the docking proteins and Pex5, also Pex7, Pex4/Pex22 and Pex25 were present in Pex14 complexes isolated from pex3 cells. However, formation of the entire importomer was not observed, most likely because Pex8 and the RING proteins were absent in the Pex14 protein complexes.Our data suggest that peroxisomal membrane vesicles can form in the absence of Pex3 and that several PMPs can insert in these vesicles in a Pex3 independent manner.

KW - peroxisome

KW - organelle

KW - Pex3

KW - peroxisomal membrane protein

KW - protein sorting

KW - endoplasmatic reticulum

KW - yeast

KW - Saccharomyces cerevisiae

U2 - 10.1016/j.bbamcr.2017.05.021

DO - 10.1016/j.bbamcr.2017.05.021

M3 - Article

VL - 1864

SP - 1656

EP - 1667

JO - Biochimica et Biophysica Acta - Molecular Cell Research

JF - Biochimica et Biophysica Acta - Molecular Cell Research

SN - 0167-4889

IS - 10

M1 - bbamcr.2017.05.021

ER -

ID: 42596760