Publication

Insights into the Role of the Peroxisomal Ubiquitination Machinery in Pex13p Degradation in the Yeast Hansenula polymorpha

Chen, X., Devarajan, S., Danda, N. & Williams, C., 25-May-2018, In : Journal of Molecular Biology. 430, 11, p. 1545-1558 14 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Chen, X., Devarajan, S., Danda, N., & Williams, C. (2018). Insights into the Role of the Peroxisomal Ubiquitination Machinery in Pex13p Degradation in the Yeast Hansenula polymorpha. Journal of Molecular Biology, 430(11), 1545-1558. https://doi.org/10.1016/j.jmb.2018.03.033

Author

Chen, Xin ; Devarajan, Srishti ; Danda, Natasha ; Williams, Chris. / Insights into the Role of the Peroxisomal Ubiquitination Machinery in Pex13p Degradation in the Yeast Hansenula polymorpha. In: Journal of Molecular Biology. 2018 ; Vol. 430, No. 11. pp. 1545-1558.

Harvard

Chen, X, Devarajan, S, Danda, N & Williams, C 2018, 'Insights into the Role of the Peroxisomal Ubiquitination Machinery in Pex13p Degradation in the Yeast Hansenula polymorpha', Journal of Molecular Biology, vol. 430, no. 11, pp. 1545-1558. https://doi.org/10.1016/j.jmb.2018.03.033

Standard

Insights into the Role of the Peroxisomal Ubiquitination Machinery in Pex13p Degradation in the Yeast Hansenula polymorpha. / Chen, Xin; Devarajan, Srishti; Danda, Natasha; Williams, Chris.

In: Journal of Molecular Biology, Vol. 430, No. 11, 25.05.2018, p. 1545-1558.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Chen X, Devarajan S, Danda N, Williams C. Insights into the Role of the Peroxisomal Ubiquitination Machinery in Pex13p Degradation in the Yeast Hansenula polymorpha. Journal of Molecular Biology. 2018 May 25;430(11):1545-1558. https://doi.org/10.1016/j.jmb.2018.03.033


BibTeX

@article{fb7e9aad35884447842af40e47720331,
title = "Insights into the Role of the Peroxisomal Ubiquitination Machinery in Pex13p Degradation in the Yeast Hansenula polymorpha",
abstract = "The import of matrix proteins into peroxisomes in yeast requires the action of the ubiquitin-conjugating enzyme Pex4p and a complex consisting of the ubiquitin E3 ligases Pex2p, Pex10p and Pex12p. Together, this peroxisomal ubiquitination machinery is thought to ubiquitinate the cycling receptor protein Pex5p and members of the Pex20p family of co-receptors, a modification that is required for receptor recycling. However, recent reports have demonstrated that this machinery plays a role in additional peroxisome-associated processes. Hence, our understanding of the function of these proteins in peroxisome biology is still incomplete. Here, we identify a role for the peroxisomal ubiquitination machinery in the degradation of the peroxisomal membrane protein Pex13p. Our data demonstrate that Pex13p levels build up in cells lacking members of this machinery and also establish that Pex13p undergoes rapid degradation in wild-type cells. Furthermore, we show that Pex13p is ubiquitinated in wild-type cells and also establish that Pex13p ubiquitination is reduced in cells lacking a functional peroxisomal E3 ligase complex. Finally, deletion of PEX2 causes Pex13p to build up at the peroxisomal membrane. Taken together, our data provide further evidence that the role of the peroxisomal ubiquitination machinery in peroxisome biology goes much deeper than receptor recycling alone.",
keywords = "IMPORT RECEPTOR PEX5P, PROTEASOME SYSTEM, MEMBRANE-PROTEINS, MATRIX PROTEIN, LIGASE SP1, SH3 DOMAIN, BIOGENESIS, SIGNAL, ARABIDOPSIS, DOCKING",
author = "Xin Chen and Srishti Devarajan and Natasha Danda and Chris Williams",
note = "Copyright {\circledC} 2018 The Author(s). Published by Elsevier Ltd.. All rights reserved.",
year = "2018",
month = "5",
day = "25",
doi = "10.1016/j.jmb.2018.03.033",
language = "English",
volume = "430",
pages = "1545--1558",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press",
number = "11",

}

RIS

TY - JOUR

T1 - Insights into the Role of the Peroxisomal Ubiquitination Machinery in Pex13p Degradation in the Yeast Hansenula polymorpha

AU - Chen, Xin

AU - Devarajan, Srishti

AU - Danda, Natasha

AU - Williams, Chris

N1 - Copyright © 2018 The Author(s). Published by Elsevier Ltd.. All rights reserved.

PY - 2018/5/25

Y1 - 2018/5/25

N2 - The import of matrix proteins into peroxisomes in yeast requires the action of the ubiquitin-conjugating enzyme Pex4p and a complex consisting of the ubiquitin E3 ligases Pex2p, Pex10p and Pex12p. Together, this peroxisomal ubiquitination machinery is thought to ubiquitinate the cycling receptor protein Pex5p and members of the Pex20p family of co-receptors, a modification that is required for receptor recycling. However, recent reports have demonstrated that this machinery plays a role in additional peroxisome-associated processes. Hence, our understanding of the function of these proteins in peroxisome biology is still incomplete. Here, we identify a role for the peroxisomal ubiquitination machinery in the degradation of the peroxisomal membrane protein Pex13p. Our data demonstrate that Pex13p levels build up in cells lacking members of this machinery and also establish that Pex13p undergoes rapid degradation in wild-type cells. Furthermore, we show that Pex13p is ubiquitinated in wild-type cells and also establish that Pex13p ubiquitination is reduced in cells lacking a functional peroxisomal E3 ligase complex. Finally, deletion of PEX2 causes Pex13p to build up at the peroxisomal membrane. Taken together, our data provide further evidence that the role of the peroxisomal ubiquitination machinery in peroxisome biology goes much deeper than receptor recycling alone.

AB - The import of matrix proteins into peroxisomes in yeast requires the action of the ubiquitin-conjugating enzyme Pex4p and a complex consisting of the ubiquitin E3 ligases Pex2p, Pex10p and Pex12p. Together, this peroxisomal ubiquitination machinery is thought to ubiquitinate the cycling receptor protein Pex5p and members of the Pex20p family of co-receptors, a modification that is required for receptor recycling. However, recent reports have demonstrated that this machinery plays a role in additional peroxisome-associated processes. Hence, our understanding of the function of these proteins in peroxisome biology is still incomplete. Here, we identify a role for the peroxisomal ubiquitination machinery in the degradation of the peroxisomal membrane protein Pex13p. Our data demonstrate that Pex13p levels build up in cells lacking members of this machinery and also establish that Pex13p undergoes rapid degradation in wild-type cells. Furthermore, we show that Pex13p is ubiquitinated in wild-type cells and also establish that Pex13p ubiquitination is reduced in cells lacking a functional peroxisomal E3 ligase complex. Finally, deletion of PEX2 causes Pex13p to build up at the peroxisomal membrane. Taken together, our data provide further evidence that the role of the peroxisomal ubiquitination machinery in peroxisome biology goes much deeper than receptor recycling alone.

KW - IMPORT RECEPTOR PEX5P

KW - PROTEASOME SYSTEM

KW - MEMBRANE-PROTEINS

KW - MATRIX PROTEIN

KW - LIGASE SP1

KW - SH3 DOMAIN

KW - BIOGENESIS

KW - SIGNAL

KW - ARABIDOPSIS

KW - DOCKING

U2 - 10.1016/j.jmb.2018.03.033

DO - 10.1016/j.jmb.2018.03.033

M3 - Article

VL - 430

SP - 1545

EP - 1558

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 11

ER -

ID: 60959560