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The endoplasmic reticulum P5A-ATPase is a transmembrane helix dislocase.

McKenna MJ, Sim SI, Ordureau A, Wei L, Harper JW, Shao S, Park E
Science 369 (2020)
Related entries: 6xmp, 6xmq, 6xms, 6xmu

Cited: 56 times
EuropePMC logo PMID: 32973005

Abstract

Organelle identity depends on protein composition. How mistargeted proteins are selectively recognized and removed from organelles is incompletely understood. Here, we found that the orphan P5A-adenosine triphosphatase (ATPase) transporter ATP13A1 (Spf1 in yeast) directly interacted with the transmembrane segment (TM) of mitochondrial tail-anchored proteins. P5A-ATPase activity mediated the extraction of mistargeted proteins from the endoplasmic reticulum (ER). Cryo-electron microscopy structures of Saccharomyces cerevisiae Spf1 revealed a large, membrane-accessible substrate-binding pocket that alternately faced the ER lumen and cytosol and an endogenous substrate resembling an α-helical TM. Our results indicate that the P5A-ATPase could dislocate misinserted hydrophobic helices flanked by short basic segments from the ER. TM dislocation by the P5A-ATPase establishes an additional class of P-type ATPase substrates and may correct mistakes in protein targeting or topogenesis.

Articles - 6xmt mentioned but not cited (3)

  1. The endoplasmic reticulum P5A-ATPase is a transmembrane helix dislocase. McKenna MJ, Sim SI, Ordureau A, Wei L, Harper JW, Shao S, Park E. Science 369 eabc5809 (2020)
  2. Structure and transport mechanism of P5B-ATPases. Li P, Wang K, Salustros N, Grønberg C, Gourdon P. Nat Commun 12 3973 (2021)
  3. Cryo-EM reveals mechanistic insights into lipid-facilitated polyamine export by human ATP13A2. Tomita A, Daiho T, Kusakizako T, Yamashita K, Ogasawara S, Murata T, Nishizawa T, Nureki O. Mol Cell 81 4799-4809.e5 (2021)


Reviews citing this publication (14)

  1. The mechanisms of integral membrane protein biogenesis. Hegde RS, Keenan RJ. Nat Rev Mol Cell Biol 23 107-124 (2022)
  2. Order through destruction: how ER-associated protein degradation contributes to organelle homeostasis. Christianson JC, Carvalho P. EMBO J 41 e109845 (2022)
  3. Capture and delivery of tail-anchored proteins to the endoplasmic reticulum. Farkas Á, Bohnsack KE. J Cell Biol 220 e202105004 (2021)
  4. ER-SURF: Riding the Endoplasmic Reticulum Surface to Mitochondria. Koch C, Schuldiner M, Herrmann JM. Int J Mol Sci 22 9655 (2021)
  5. Fidelity of Cotranslational Protein Targeting to the Endoplasmic Reticulum. Hsieh HH, Shan SO. Int J Mol Sci 23 281 (2021)
  6. Membrane protein folding and quality control. Phillips BP, Miller EA. Curr Opin Struct Biol 69 50-54 (2021)
  7. Protein Quality Control at the Mitochondrial Surface. den Brave F, Gupta A, Becker T. Front Cell Dev Biol 9 795685 (2021)
  8. The Molecular Biodiversity of Protein Targeting and Protein Transport Related to the Endoplasmic Reticulum. Tirincsi A, Sicking M, Hadzibeganovic D, Haßdenteufel S, Lang S. Int J Mol Sci 23 143 (2021)
  9. The Roles of ATP13A2 Gene Mutations Leading to Abnormal Aggregation of α-Synuclein in Parkinson's Disease. Zhang F, Wu Z, Long F, Tan J, Gong N, Li X, Lin C. Front Cell Neurosci 16 927682 (2022)
  10. Cell death induction in Aspergillus fumigatus: accentuating drug toxicity through inhibition of the unfolded protein response (UPR). Guirao-Abad JP, Weichert M, Askew DS. Curr Res Microb Sci 3 100119 (2022)
  11. Cryo-EM structures of the endoplasmic reticulum membrane complex. Bai L, Li H. FEBS J 289 102-112 (2022)
  12. P-type ATPases: Many more enigmas left to solve. Palmgren M. J Biol Chem 299 105352 (2023)
  13. Spf1 and Ste24: quality controllers of transmembrane protein topology in the eukaryotic cell. Tipper DJ, Harley CA. Front Cell Dev Biol 11 1220441 (2023)
  14. MR1 antigen presentation to MAIT cells and other MR1-restricted T cells. McWilliam HEG, Villadangos JA. Nat Rev Immunol (2023)

Articles citing this publication (39)



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