Publications by authors named "Renate Maier"

Article Synopsis
  • Peroxisomes are essential organelles involved in metabolism, and their dysfunction can lead to human diseases; their proper functioning requires the import of specific proteins tagged with a peroxisomal targeting signal (PTS) 1.
  • The receptor protein Pex5p is responsible for recruiting these PTS1-proteins for import, and the study identifies 22 phosphorylation sites on Pex5p that may regulate this process post-translationally.
  • The research shows that phospho-mimicking mutations in Pex5p decrease its ability to import certain PTS1-proteins, revealing a new mechanism where phosphorylation affects protein binding and cargo import, thereby influencing peroxisomal composition and overall metabolism.
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Peroxisomes and the endoplasmic reticulum (ER) cooperate in cellular lipid metabolism. They form membrane contacts through interaction of the peroxisomal membrane protein ACBD5 (acyl-coenzyme A-binding domain protein 5) and the ER-resident protein VAPB (vesicle-associated membrane protein-associated protein B). ACBD5 binds to the major sperm protein domain of VAPB via its FFAT-like (two phenylalanines [FF] in an acidic tract) motif.

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The peroxisomal biogenesis factor Pex14p is an essential component of the peroxisomal matrix protein import machinery. Together with Pex13p and Pex17p, it is part of the membrane-associated peroxisomal docking complex in yeast, facilitating the binding of cargo-loaded receptor proteins for translocation of cargo proteins into the peroxisome. Furthermore, Pex14p is part of peroxisomal import pores.

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Trypanosomatid parasites cause devastating African sleeping sickness, Chagas disease, and Leishmaniasis that affect about 18 million people worldwide. Recently, we showed that the biogenesis of glycosomes could be the "Achilles' heel" of trypanosomatids suitable for the development of new therapies against trypanosomiases. This was shown for inhibitors of the import machinery of matrix proteins, while the distinct machinery for the topogenesis of glycosomal membrane proteins evaded investigation due to the lack of a druggable interface.

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