Pex24 and Pex32 are required to tether peroxisomes to the ER for organelle biogenesis, positioning and segregation in yeast

Wu, Fei; Boer, Rinse de; Krikken, Arjen M; Akşit, Arman; Bordin, Nicola; Devos, Damien P.; Klei, Ida J. van der

doi:10.1242/jcs.246983

Cited by 26 publications

(74 citation statements)

References 58 publications

(90 reference statements)

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“…3 D). In line with our earlier observations, peroxisome-ER contacts require Pex32 (Wu et al, 2020). The distance between peroxisomes and ER increased in the absence of Pex32, whereas associations with the PM were unaffected in these cells (Fig.…”

Section: Inp1 Colocalizes With Pex3 At Peroxisome-pm Contactssupporting

confidence: 93%

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

Krikken

Boer

et al. 2020

Journal of Cell Biology

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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.

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Section: Inp1 Colocalizes With Pex3 At Peroxisome-pm Contactssupporting

confidence: 93%

“…Pyc1 was used as a loading control. contact sites (Wu et al, 2020). To analyze the contribution of ER and PM contact sites, we compared peroxisome inheritance in inp1, pex32, and inp1 pex32 strains.…”

Section: Inp1 Colocalizes With Pex3 At Peroxisome-pm Contactsmentioning

confidence: 99%

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

Krikken

Boer

et al. 2020

Journal of Cell Biology

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“…interplay and membrane contacts have also been reported (van Roermund et al, 2000;Dulermo et al, 2015;Mattiazzi Ušaj et al, 2015;Mindthoff et al, 2016;Kustatscher et al, 2019;Wu et al, 2020).…”

Section: Discussionmentioning

confidence: 82%

A Functional SMAD2/3 Binding Site in the PEX11β Promoter Identifies a Role for TGFβ in Peroxisome Proliferation in Humans

Azadi

Carmichael

Kovacs

et al. 2020

Front. Cell Dev. Biol.

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In mammals, peroxisomes perform crucial functions in cellular metabolism, signaling and viral defense which are essential to the viability of the organism. Molecular cues triggered by changes in the cellular environment induce a dynamic response in peroxisomes, which manifests itself as a change in peroxisome number, altered enzyme levels and adaptations to the peroxisomal morphology. How the regulation of this process is integrated into the cell's response to different stimuli, including the signaling pathways and factors involved, remains unclear. Here, a cell-based peroxisome proliferation assay has been applied to investigate the ability of different stimuli to induce peroxisome proliferation. We determined that serum stimulation, long-chain fatty acid supplementation and TGFβ application all increase peroxisome elongation, a prerequisite for proliferation. Time-resolved mRNA expression during the peroxisome proliferation cycle revealed a number of peroxins whose expression correlated with peroxisome elongation, including the β isoform of PEX11, but not the α or γ isoforms. An initial map of putative regulatory motif sites in the respective promoters showed a difference between binding sites in PEX11α and PEX11β, suggesting that these genes may be regulated by distinct pathways. A functional SMAD2/3 binding site in PEX11β points to the involvement of the TGFβ signaling pathway in expression of this gene and thus peroxisome proliferation/dynamics in humans.

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“…Although initially reported at the peroxisome (Brown et al, 2000, Tam & Rachubinski, 2002, Vizeacoumar et al, 2003, Vizeacoumar et al, 2004), later studies either reported dual localization to peroxisomes and ER (David et al, 2013, Yan et al, 2008) or exclusive localization at ER subdomains (Joshi et al, 2016, Mast et al, 2016, Wu et al, 2020). A recent study characterizing O. polymorpha Pex23 family members reported the involvement of PEX24 and PEX32 in peroxisome- ER contact sites (Wu et al, 2020). This could explain the previous contradictory reports on their localization, as they can be expected to be present in spots where peroxisomes and ER interact.…”

Section: Resultsmentioning

confidence: 99%

“…O. polymorpha PEX11 has been implicated in peroxisome segregation during cell division (Krikken et al, 2009). S. cerevisiae PEX11 and PEX34 are involved in peroxisome-mitochondria contact sites (Shai et al, 2018, Ušaj et al, 2015), while O. polymorpha PEX11 has been implicated in peroxisome-ER contact sites (Wu et al, 2020). S. cerevisiae PEX11 has also been proposed to act as a pore-forming protein (Mindthoff et al, 2016) and has been implicated in medium chain fatty acid oxidation as well (van Roermund et al, 2000).…”

Section: Resultsmentioning

confidence: 99%

Comparative genomics of peroxisome biogenesis proteins: making sense of the PEX mess

Jansen

Molina

Noort

et al. 2020

Preprint

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PEX genes encode proteins involved in peroxisome biogenesis and proliferation. Using a comparative genomics approach, we clarify the evolutionary relationships between the 37 known PEX proteins in a representative set of eukaryotes, including all common model organisms, pathogenic unicellular eukaryotes and human. A large number of previously unknown PEX orthologs were identified. We analysed all PEX proteins, their conservation and domain architecture and defined the minimum set of PEX proteins that is required to make a peroxisome. The molecular processes in peroxisome biogenesis in different organisms were put into context, showing that peroxisomes are not static organelles in eukaryotic evolution. Organisms that lack peroxisomes still contain a few PEX proteins, which probably play a role in alternative processes. Finally, the relationships between PEX proteins of two large families, the Pex11 and Pex23 families, were clarified, thereby contributing to the understanding of their complicated and sometimes incorrect nomenclature. We provide an exhaustive overview of this important eukaryotic organelle.

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Pex24 and Pex32 are required to tether peroxisomes to the ER for organelle biogenesis, positioning and segregation in yeast

Cited by 26 publications

References 58 publications

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

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

A Functional SMAD2/3 Binding Site in the PEX11β Promoter Identifies a Role for TGFβ in Peroxisome Proliferation in Humans

Comparative genomics of peroxisome biogenesis proteins: making sense of the PEX mess

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