FMP Publications

Our publications are recorded in a searchable database since 2010, updates will be added regularly.

All :: 2015
All :: (, A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z 
All :: O'Connor(*), ... , Oosterhof(*), Opalinski(*), Opitz, ... , Ozdogan(*) 
References per page: Show keywords Show abstracts
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.
Proc Natl Acad Sci U S A, 112:6377-6382

Tags: Peptide Synthesis (Hackenberger/Volkmer)

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 Pex11beta 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.

Export as:

Leibniz-Forschungsinstitut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP)
Campus Berlin-Buch
Robert-Roessle-Str. 10
13125 Berlin, Germany
+4930 94793 - 100 
+4930 94793 - 109 (Fax)

Like many sites, we use cookies to optimize the user's browsing experience. Data Protection OK