Peroxisome retention involves Inp1-dependent peroxisome-plasma membrane contact sites in yeast

Arjen M Krikken, Huala Wu, Rinse de Boer, Damien P Devos, Tim P Levine, Ida J van der Klei*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

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Abstract

Retention of peroxisomes in yeast mother cells requires Inp1, which is recruited to the organelle by the peroxisomal membrane protein Pex3. Here we show that Hansenula polymorpha Inp1 associates peroxisomes to the plasma membrane. Peroxisome-plasma membrane contact sites disappear upon deletion of INP1 but increase upon INP1 overexpression. Analysis of truncated Inp1 variants showed that the C terminus is important for association to the peroxisome, while a stretch of conserved positive charges and a central pleckstrin homology-like domain are important for plasma membrane binding. In cells of a PEX3 deletion, strain Inp1-GFP localizes to the plasma membrane, concentrated in patches near the bud neck and in the cortex of nascent buds. Upon disruption of the actin cytoskeleton by treatment of the cells with latrunculin A, Inp1-GFP became cytosolic, indicating that Inp1 localization is dependent on the presence of an intact actin cytoskeleton.

Original languageEnglish
Article numbere201906023
Number of pages11
JournalThe Journal of Cell Biology
Volume219
Issue number10
DOIs
Publication statusPublished - 5-Oct-2020

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