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Ida J. Van Der Klei  - - - 
Publication Record
Distribution of Articles published per year 
(1991 - 2016)
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Article 0 Reads 0 Citations Peroxisomes: new insights into protein sorting, dynamics, quality control, signalling and roles in health and disease Joseph L. Costello, Einat Zalckvar, Stephan Kemp, Francesca ... Published: 29 March 2019
Histochemistry and Cell Biology, doi: 10.1007/s00418-019-01780-w
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Article 0 Reads 4 Citations Assembly of the Mitochondrial Cristae Organizer Mic10 Is Regulated by Mic26–Mic27 Antagonism and Cardiolipin Heike Rampelt, Florian Wollweber, Carolin Gerke, Rinse De Bo... Published: 01 June 2018
Journal of Molecular Biology, doi: 10.1016/j.jmb.2018.04.037
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Article 0 Reads 5 Citations Yeast cells contain a heterogeneous population of peroxisomes that segregate asymmetrically during cell division Sanjeev Kumar, Rinse De Boer, Ida J. Van Der Klei Published: 21 December 2017
Journal of Cell Science, doi: 10.1242/jcs.207522
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Article 0 Reads 6 Citations Saccharomyces cerevisiae cells lacking Pex3 contain membrane vesicles that harbor a subset of peroxisomal membrane prote... Justyna P. Wróblewska, Luis Daniel Cruz-Zaragoza, Wei Yuan, ... Published: 01 October 2017
Biochimica et Biophysica Acta (BBA) - Bioenergetics, doi: 10.1016/j.bbamcr.2017.05.021
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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 Pex11 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.
Article 0 Reads 0 Citations Impaired biosynthesis of the non-bilayer lipids phosphatidylethanolamine or cardiolipin does not affect peroxisome bioge... Adam Kawałek, Chandhuru Jagadeesan, Ida J. Van Der Klei Published: 01 November 2016
Biochemical and Biophysical Research Communications, doi: 10.1016/j.bbrc.2016.10.033
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Article 0 Reads 3 Citations The birth of yeast peroxisomes Wei Yuan, Marten Veenhuis, Ida J. Van Der Klei Published: 01 May 2016
Biochimica et Biophysica Acta (BBA) - Bioenergetics, doi: 10.1016/j.bbamcr.2015.09.008
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This contribution describes the phenotypic differences of yeast peroxisome-deficient mutants (pex mutants). In some cases different phenotypes were reported for yeast mutants deleted in the same PEX gene. These differences are most likely related to the marker proteins and methods used to detect peroxisomal remnants. This is especially evident for pex3 and pex19 mutants, where the localization of receptor docking proteins (Pex13, Pex14) resulted in the identification of peroxisomal membrane remnants, which do not contain other peroxisomal membrane proteins, such as the ring proteins Pex2, Pex10 and Pex12. These structures in pex3 and pex19 cells are the template for peroxisome formation upon introduction of the missing gene. Taken together, these data suggest that in all yeast pex mutants analyzed so far peroxisomes are not formed de novo but use membrane remnant structures as a template for peroxisome formation upon reintroduction of the missing gene. The relevance of this model for peroxisomal membrane protein and lipid sorting to peroxisomes is discussed.