Novel targeting assay uncovers targeting information within peroxisomal ABC transporter Pxa1

Jansen, Renate; Noort, Marco van den; Krikken, Arjen M; Bibi, Chen; Böhm, Astrid; Schuldiner, Maya; Zalckvar, Einat; Klei, Ida J. van der

doi:10.1016/j.bbamcr.2023.119471

Cited by 1 publication

(1 citation statement)

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“…Along this line, the N-terminal 95 residues of Pxa1p have recently been shown to be sufficient for targeting a reporter protein to peroxisomes. Interestingly, truncated Pxa1p lacking residues 1–95 still localized to peroxisomes but its targeting depended on the presence of its interaction partner Pxa2 ( Jansen et al, 2023 ).…”

Section: Discussionmentioning

confidence: 99%

Molecular basis of the glycosomal targeting of PEX11 and its mislocalization to mitochondrion in trypanosomes

Krishna,

Schmidt,

Tippler

et al. 2023

Front. Cell Dev. Biol.

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PEX19 binding sites are essential parts of the targeting signals of peroxisomal membrane proteins (mPTS). In this study, we characterized PEX19 binding sites of PEX11, the most abundant peroxisomal and glycosomal membrane protein from Trypanosoma brucei and Saccharomyces cerevisiae. TbPEX11 contains two PEX19 binding sites, one close to the N-terminus (BS1) and a second in proximity to the first transmembrane domain (BS2). The N-terminal BS1 is highly conserved across different organisms and is required for maintenance of the steady-state concentration and efficient targeting to peroxisomes and glycosomes in both baker’s yeast and Trypanosoma brucei. The second PEX19 binding site in TbPEX11 is essential for its glycosomal localization. Deletion or mutations of the PEX19 binding sites in TbPEX11 or ScPEX11 results in mislocalization of the proteins to mitochondria. Bioinformatic analysis indicates that the N-terminal region of TbPEX11 contains an amphiphilic helix and several putative TOM20 recognition motifs. We show that the extreme N-terminal region of TbPEX11 contains a cryptic N-terminal signal that directs PEX11 to the mitochondrion if its glycosomal transport is blocked.

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Section: Discussionmentioning

confidence: 99%