scholarly journals Pex24 and Pex32 tether peroxisomes to the ER for organelle biogenesis, positioning and segregation

2020 ◽  
Author(s):  
Fei Wu ◽  
Rinse de Boer ◽  
Arjen M. Krikken ◽  
Arman Akşit ◽  
Nicola Bordin ◽  
...  

AbstractWe analyzed all four Pex23 family proteins of the yeast Hansenula polymorpha, which localize to the ER. Of these Pex24 and Pex32, but not Pex23 and Pex29, accumulate at peroxisome-ER contacts, where they are important for normal peroxisome biogenesis and proliferation and contribute to organelle positioning and segregation.Upon deletion of PEX24 and PEX32 - and to a lesser extent of PEX23 and PEX29 - peroxisome-ER contacts are disrupted, concomitant with peroxisomal defects. These defects are suppressed upon introduction of an artificial peroxisome-ER tether.Accumulation of Pex32 at peroxisomes-ER contacts is lost in the absence of the peroxisomal membrane protein Pex11. At the same time peroxisome-ER contacts are disrupted, indicating that Pex11 contributes to Pex32-dependent peroxisome-ER contact formation.Summarizing, our data indicate that H. polymorpha Pex24 and Pex32 are tethers at peroxisome-ER contacts that are important for normal peroxisome biogenesis and dynamics.SummaryTwo Hansenula polymorpha ER proteins, Pex24 and Pex32, are tethers at peroxisome-ER contacts and function together with the peroxisomal protein Pex11. Their absence disturbs these contacts leading to multiple peroxisomal defects, which can be restored by an artificial tether.

2020 ◽  
Vol 133 (16) ◽  
pp. jcs246983 ◽  
Author(s):  
Fei Wu ◽  
Rinse de Boer ◽  
Arjen M. Krikken ◽  
Arman Akşit ◽  
Nicola Bordin ◽  
...  

ABSTRACTThe yeast Hansenula polymorpha contains four members of the Pex23 family of peroxins, which characteristically contain a DysF domain. Here we show that all four H. polymorpha Pex23 family proteins localize to the endoplasmic reticulum (ER). Pex24 and Pex32, but not Pex23 and Pex29, predominantly accumulate at peroxisome–ER contacts. Upon deletion of PEX24 or PEX32 – and to a much lesser extent, of PEX23 or PEX29 – peroxisome–ER contacts are lost, concomitant with defects in peroxisomal matrix protein import, membrane growth, and organelle proliferation, positioning and segregation. These defects are suppressed by the introduction of an artificial peroxisome–ER tether, indicating that Pex24 and Pex32 contribute to tethering of peroxisomes to the ER. Accumulation of Pex32 at these contact sites is lost in cells lacking the peroxisomal membrane protein Pex11, in conjunction with disruption of the contacts. This indicates that Pex11 contributes to Pex32-dependent peroxisome–ER contact formation. The absence of Pex32 has no major effect on pre-peroxisomal vesicles that occur in pex3 atg1 deletion cells.


1996 ◽  
Vol 271 (31) ◽  
pp. 18973-18980 ◽  
Author(s):  
Erik A. C. Wiemer ◽  
Georg H. Lüers ◽  
Klaas Nico Faber ◽  
Thibaut Wenzel ◽  
Marten Veenhuis ◽  
...  

FEBS Journal ◽  
2019 ◽  
Vol 287 (9) ◽  
pp. 1742-1757 ◽  
Author(s):  
Ritika Singh ◽  
Selvambigai Manivannan ◽  
Arjen M. Krikken ◽  
Rinse Boer ◽  
Nicola Bordin ◽  
...  

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