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TitleATP13A1 engages SEC61 to facilitate substrate-specific translocation.
Journal, issue, pagesSci Adv, Vol. 11, Issue 24, Page eadt1346, Year 2025
Publish dateJun 13, 2025
AuthorsXiaoyan Yang / Yi Li / Chengxi Yang / Tingting Li / Zhiyu Fang / Zhigang Feng / Jun Liao / Yan Zou /
PubMed AbstractThe accurate targeting of proteins to their designated cellular compartments is essential for maintaining proper cellular architecture and function. However, interpreting and sorting the highly ...The accurate targeting of proteins to their designated cellular compartments is essential for maintaining proper cellular architecture and function. However, interpreting and sorting the highly variable targeting sequences in secreted and membrane proteins present a substantial challenge for achieving precise localization within the secretory pathway. In this study, we demonstrate that atypical signal sequences, characterized by high hydrophobicity and/or the absence of characteristic charges, are recognized by the signal recognition particle and targeted to the endoplasmic reticulum in a reverse orientation. These misoriented signal sequences are subsequently dislocated by the P5A-ATPase ATP13A1 and delivered to SEC61 for further translocation. Using cryo-electron microscopy, we determined the structures of human ATP13A1 in multiple conformations (3.40- to 3.87-angstrom resolution), revealing key residues within its substrate-binding pocket that engage signal sequences through polar interactions. Collectively, our findings elucidate a comprehensive, substrate-specific translocation pathway that ensures both high efficiency and fidelity in protein subcellular localization.
External linksSci Adv / PubMed:40498833 / PubMed Central
MethodsEM (single particle)
Resolution3.4 - 3.87 Å
Structure data

61319

9jbm

EMDB-61319, PDB-9jbm:
P5A-ATPase ATP13A1 reconstructed in nanodiscs
Method: EM (single particle) / Resolution: 3.83 Å

61323

9jbr

EMDB-61323, PDB-9jbr:
P5A-ATPase ATP13A1 D533N mutant
Method: EM (single particle) / Resolution: 3.4 Å

61329

9jbx

EMDB-61329, PDB-9jbx:
P5A-ATPase ATP13A1 in E1P state
Method: EM (single particle) / Resolution: 3.87 Å

61331

9jbz

EMDB-61331, PDB-9jbz:
P5A-ATPase ATP13A1 in E2P state
Method: EM (single particle) / Resolution: 3.67 Å

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / ER membrane / Transmembrane helices / Translocation / Mutant / E1P state / E2P state

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