AUTHOR=Wu Fei , van der Klei Ida J. 

TITLE=Structure–function analysis of the ER-peroxisome contact site protein Pex32

JOURNAL=Frontiers in Cell and Developmental Biology

VOLUME=10

YEAR=2022

URL=https://www.frontiersin.org/journals/cell-and-developmental-biology/articles/10.3389/fcell.2022.957871

DOI=10.3389/fcell.2022.957871

ISSN=2296-634X

ABSTRACT=<p>In the yeast <italic>Hansenula polymorpha</italic>, the ER protein Pex32 is required for associating peroxisomes to the ER. Here, we report on a structure–function analysis of Pex32. Localization studies of various Pex32 truncations showed that the N-terminal transmembrane domain of Pex32 is responsible for sorting. Moreover, this part of the protein is sufficient for the function of Pex32 in peroxisome biogenesis. The C-terminal DysF domain is required for concentrating Pex32 at ER-peroxisome contact sites and has the ability to bind to peroxisomes. In order to better understand the role of Pex32 in peroxisome biogenesis, we analyzed various peroxisomal proteins in <italic>pex32</italic> cells. This revealed that Pex11 levels are strongly reduced in <italic>pex32</italic> cells. This may explain the strong reduction in peroxisome numbers in <italic>pex32</italic> cells, which also occurs in cells lacking Pex11.</p>