Publication

The membrane remodeling protein Pex11p activates the GTPase Dnm1p during peroxisomal fission

Williams, C., Opalinski, L., Landgraf, C., Costello, J., Schrader, M., Krikken, A. M., Knoops, K., Kram, A. M., Volkmer, R. & van der Klei, I. J., 4-May-2015, In : Proceedings of the National Academy of Sciences of the United States of America. 112, 20, p. 6377-6382 6 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Williams, C., Opalinski, L., Landgraf, C., Costello, J., Schrader, M., Krikken, A. M., ... van der Klei, I. J. (2015). The membrane remodeling protein Pex11p activates the GTPase Dnm1p during peroxisomal fission. Proceedings of the National Academy of Sciences of the United States of America, 112(20), 6377-6382. https://doi.org/10.1073/pnas.1418736112

Author

Williams, Chris ; Opalinski, Lukasz ; Landgraf, Christiane ; Costello, Joseph ; Schrader, Michael ; Krikken, Arjen M ; Knoops, Kèvin ; Kram, Anita M ; Volkmer, Rudolf ; van der Klei, Ida J. / The membrane remodeling protein Pex11p activates the GTPase Dnm1p during peroxisomal fission. In: Proceedings of the National Academy of Sciences of the United States of America. 2015 ; Vol. 112, No. 20. pp. 6377-6382.

Harvard

Williams, C, Opalinski, L, Landgraf, C, Costello, J, Schrader, M, Krikken, AM, Knoops, K, Kram, AM, Volkmer, R & van der Klei, IJ 2015, 'The membrane remodeling protein Pex11p activates the GTPase Dnm1p during peroxisomal fission', Proceedings of the National Academy of Sciences of the United States of America, vol. 112, no. 20, pp. 6377-6382. https://doi.org/10.1073/pnas.1418736112

Standard

The membrane remodeling protein Pex11p activates the GTPase Dnm1p during peroxisomal fission. / Williams, Chris; Opalinski, Lukasz; Landgraf, Christiane; Costello, Joseph; Schrader, Michael; Krikken, Arjen M; Knoops, Kèvin; Kram, Anita M; Volkmer, Rudolf; van der Klei, Ida J.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 112, No. 20, 04.05.2015, p. 6377-6382.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Williams C, Opalinski L, Landgraf C, Costello J, Schrader M, Krikken AM et al. The membrane remodeling protein Pex11p activates the GTPase Dnm1p during peroxisomal fission. Proceedings of the National Academy of Sciences of the United States of America. 2015 May 4;112(20):6377-6382. https://doi.org/10.1073/pnas.1418736112


BibTeX

@article{8b7f3141dda04cdfa321b1699fec0e7d,
title = "The membrane remodeling protein Pex11p activates the GTPase Dnm1p during peroxisomal fission",
abstract = "The initial phase of peroxisomal fission requires the peroxisomal membrane protein Peroxin 11 (Pex11p), which remodels the membrane, resulting in organelle elongation. Here, we identify an additional function for Pex11p, demonstrating that Pex11p also plays a crucial role in the final step of peroxisomal fission: dynamin-like protein (DLP)-mediated membrane scission. First, we demonstrate that yeast Pex11p is necessary for the function of the GTPase Dynamin-related 1 (Dnm1p) in vivo. In addition, our data indicate that Pex11p physically interacts with Dnm1p and that inhibiting this interaction compromises peroxisomal fission. Finally, we demonstrate that Pex11p functions as a GTPase activating protein (GAP) for Dnm1p in vitro. Similar observations were made for mammalian Pex11β and the corresponding DLP Drp1, indicating that DLP activation by Pex11p is conserved. Our work identifies a previously unknown requirement for a GAP in DLP function.",
author = "Chris Williams and Lukasz Opalinski and Christiane Landgraf and Joseph Costello and Michael Schrader and Krikken, {Arjen M} and K{\`e}vin Knoops and Kram, {Anita M} and Rudolf Volkmer and {van der Klei}, {Ida J}",
year = "2015",
month = "5",
day = "4",
doi = "10.1073/pnas.1418736112",
language = "English",
volume = "112",
pages = "6377--6382",
journal = "Proceedings of the National Academy of Science of the United States of America",
issn = "0027-8424",
publisher = "NATL ACAD SCIENCES",
number = "20",

}

RIS

TY - JOUR

T1 - The membrane remodeling protein Pex11p activates the GTPase Dnm1p during peroxisomal fission

AU - Williams, Chris

AU - Opalinski, Lukasz

AU - Landgraf, Christiane

AU - Costello, Joseph

AU - Schrader, Michael

AU - Krikken, Arjen M

AU - Knoops, Kèvin

AU - Kram, Anita M

AU - Volkmer, Rudolf

AU - van der Klei, Ida J

PY - 2015/5/4

Y1 - 2015/5/4

N2 - The initial phase of peroxisomal fission requires the peroxisomal membrane protein Peroxin 11 (Pex11p), which remodels the membrane, resulting in organelle elongation. Here, we identify an additional function for Pex11p, demonstrating that Pex11p also plays a crucial role in the final step of peroxisomal fission: dynamin-like protein (DLP)-mediated membrane scission. First, we demonstrate that yeast Pex11p is necessary for the function of the GTPase Dynamin-related 1 (Dnm1p) in vivo. In addition, our data indicate that Pex11p physically interacts with Dnm1p and that inhibiting this interaction compromises peroxisomal fission. Finally, we demonstrate that Pex11p functions as a GTPase activating protein (GAP) for Dnm1p in vitro. Similar observations were made for mammalian Pex11β and the corresponding DLP Drp1, indicating that DLP activation by Pex11p is conserved. Our work identifies a previously unknown requirement for a GAP in DLP function.

AB - The initial phase of peroxisomal fission requires the peroxisomal membrane protein Peroxin 11 (Pex11p), which remodels the membrane, resulting in organelle elongation. Here, we identify an additional function for Pex11p, demonstrating that Pex11p also plays a crucial role in the final step of peroxisomal fission: dynamin-like protein (DLP)-mediated membrane scission. First, we demonstrate that yeast Pex11p is necessary for the function of the GTPase Dynamin-related 1 (Dnm1p) in vivo. In addition, our data indicate that Pex11p physically interacts with Dnm1p and that inhibiting this interaction compromises peroxisomal fission. Finally, we demonstrate that Pex11p functions as a GTPase activating protein (GAP) for Dnm1p in vitro. Similar observations were made for mammalian Pex11β and the corresponding DLP Drp1, indicating that DLP activation by Pex11p is conserved. Our work identifies a previously unknown requirement for a GAP in DLP function.

U2 - 10.1073/pnas.1418736112

DO - 10.1073/pnas.1418736112

M3 - Article

VL - 112

SP - 6377

EP - 6382

JO - Proceedings of the National Academy of Science of the United States of America

JF - Proceedings of the National Academy of Science of the United States of America

SN - 0027-8424

IS - 20

ER -

ID: 19579747