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

Chris Williams, Lukasz Opalinski, Christiane Landgraf, Joseph Costello, Michael Schrader, Arjen M Krikken, Kèvin Knoops, Anita M Kram, Rudolf Volkmer, Ida J van der Klei

Research output: Contribution to journalArticleAcademicpeer-review

43 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)6377-6382
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume112
Issue number20
DOIs
Publication statusPublished - 4-May-2015

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