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A dual role of the conserved PEX19 helix in safeguarding peroxisomal membrane proteins

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Title
A dual role of the conserved PEX19 helix in safeguarding peroxisomal membrane proteins
Author(s)
Jeonghyun Oh; Do Kyung Kim; Seung Hae Ahn; Ho Min Kim; Hyunju Cho
Publication Date
2024-04
Journal
iScience, v.27, no.4
Publisher
CELL PRESS
Abstract
Accurate localization of membrane proteins is essential for proper cellular functioning and the integrity of cellular membranes. Post-translational targeting of peroxisomal membrane proteins (PMPs) is mediated by the cytosolic chaperone PEX19 and its membrane receptor PEX3. However, the molecular mechanisms underlying PMP targeting are poorly understood. Here, using biochemical and mass spectrometry analysis, we find that a conserved PEX19 helix, αd, is critical to prevent improper exposure of the PEX26 transmembrane domain (TMD) to cytosolic chaperones. Furthermore, the αd helix of PEX19 interacts with the cytosolic domain of the PEX3 receptor, thereby triggering PEX26 release at the correct destination membrane. The peroxisome-deficient PEX3-G138E mutant completely abolishes this secondary interaction, leading to lack of PEX3-induced PEX26 release from PEX19. These findings elucidate a dual molecular mechanism that is essential to membrane protein protection and destination-specific release by a molecular chaperone. © 2024 The Author(s)
URI
https://pr.ibs.re.kr/handle/8788114/15073
DOI
10.1016/j.isci.2024.109537
Appears in Collections:
Pioneer Research Center for Biomolecular and Cellular Structure(바이오분자 및 세포구조 연구단) > Protein Communication Group(단백질 커뮤니케이션 그룹) > 1. Journal Papers (저널논문)
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