An ATP13A1-assisted topogenesis pathway for folding multi-spanning membrane proteins

Ji, Jia; Cui, Meng-Ke; Zou, Rong; Wu, Ming-Zhi; Ge, Man-Xi; Li, Jiqiang; Zhang, Zai-Rong

doi:10.1016/j.molcel.2024.04.010

Molecular Cell

2024

DOI: 10.1016/j.molcel.2024.04.010

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An ATP13A1-assisted topogenesis pathway for folding multi-spanning membrane proteins

Jia Ji,

Meng-Ke Cui,

Rong Zou

et al.

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Cited by 2 publications

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Getting membrane proteins into shape

Hegde

2024

Molecular Cell

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Getting membrane proteins into shape

Hegde

2024

Molecular Cell

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The structure and function of P5A-ATPases

Li,

Bågenholm,

Hägglund

et al. 2024

Nat Commun

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Endoplasmic reticulum (ER) membrane resident P5A-ATPases broadly affect protein biogenesis and quality control, and yet their molecular function remains debated. Here, we report cryo-EM structures of a P5A-ATPase, CtSpf1, covering multiple transport intermediates of the E1 → E1-ATP → E1P-ADP → E1P → E2P → E2.Pi → E2 → E1 cycle. In the E2P and E2.Pi states a cleft spans the entire membrane, holding a polypeptide cargo molecule. The cargo includes an ER luminal extension, pinpointed as the C-terminus in the E2.Pi state, which reenters the membrane in E2P. The E1 structure harbors a cytosol-facing cavity that is blocked by an insertion we refer to as the Plug-domain. The Plug-domain is nestled to key ATPase features and is displaced in the E1P-ADP and E1P states. Collectively, our findings are compatible with a broad range of proteins as cargo, with the P5A-ATPases serving a role in membrane removal of helices, although insertion/secretion cannot be excluded, as well as with a mechanistic role of the Plug-domain.

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An ATP13A1-assisted topogenesis pathway for folding multi-spanning membrane proteins

Cited by 2 publications

References 72 publications

Getting membrane proteins into shape

Getting membrane proteins into shape

The structure and function of P5A-ATPases

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