Hydrophobic handoff for direct delivery of peroxisome tail-anchored proteins

Yinxiao Chen, Laurent Pieuchot, Rachel Ann Loh, Jing Yang, Teuku Mahfuzh Aufar Kari, Jie Yun Wong and Gregory Jedd ()
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Yinxiao Chen: Temasek Life Sciences Laboratory, National University of Singapore
Laurent Pieuchot: Temasek Life Sciences Laboratory, National University of Singapore
Rachel Ann Loh: Temasek Life Sciences Laboratory, National University of Singapore
Jing Yang: Temasek Life Sciences Laboratory, National University of Singapore
Teuku Mahfuzh Aufar Kari: Temasek Life Sciences Laboratory, National University of Singapore
Jie Yun Wong: Temasek Life Sciences Laboratory, National University of Singapore
Gregory Jedd: Temasek Life Sciences Laboratory, National University of Singapore

Nature Communications, 2014, vol. 5, issue 1, 1-12

Abstract: Abstract Tail-anchored (TA) proteins are inserted into membranes post-translationally through a C-terminal transmembrane domain (TMD). The PEX19 protein binds peroxisome TA proteins in the cytoplasm and delivers them to the membrane through the PEX3 receptor protein. An amphipathic segment in PEX19 promotes docking on PEX3. However, how this leads to substrate insertion is unknown. Here we reconstitute peroxisome TA protein biogenesis into two sequential steps of substrate TMD engagement and membrane insertion. We identify a series of previously uncharacterized amphipathic segments in PEX19 and identify one whose hydrophobicity is required for membrane insertion, but not TMD chaperone activity or PEX3 binding. A membrane-proximal hydrophobic surface of PEX3 promotes an unconventional form of membrane intercalation, and is also required for TMD insertion. Together, these data support a mechanism in which hydrophobic moieties in the TMD chaperone and its membrane-associated receptor act in a concerted manner to prompt TMD release and membrane insertion.

Date: 2014
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DOI: 10.1038/ncomms6790

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