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- W3083256367 abstract "Mitochondrial function depends on the efficient import of proteins synthesized in the cytosol. When cells experience stress, the efficiency and faithfulness of the mitochondrial protein import machinery are compromised, leading to homeostatic imbalances and damage to the organelle. Yeast Msp1 (mitochondrial sorting of proteins 1) and mammalian ATAD1 (ATPase family AAA domain–containing 1) are orthologous AAA proteins that, fueled by ATP hydrolysis, recognize and extract mislocalized membrane proteins from the outer mitochondrial membrane. Msp1 also extracts proteins that have become stuck in the import channel. The extracted proteins are targeted for proteasome-dependent degradation or, in the case of mistargeted tail-anchored proteins, are given another chance to be routed correctly. In addition, ATAD1 is implicated in the regulation of synaptic plasticity, mediating the release of neurotransmitter receptors from postsynaptic scaffolds to allow their trafficking. Here we discuss how structural and functional specialization imparts the unique properties that allow Msp1/ATAD1 ATPases to fulfill these diverse functions and also highlight outstanding questions in the field." @default.
- W3083256367 created "2020-09-11" @default.
- W3083256367 creator A5028859676 @default.
- W3083256367 creator A5087493059 @default.
- W3083256367 date "2020-10-06" @default.
- W3083256367 modified "2023-10-14" @default.
- W3083256367 title "Msp1/ATAD1 in Protein Quality Control and Regulation of Synaptic Activities" @default.
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- W3083256367 doi "https://doi.org/10.1146/annurev-cellbio-031220-015840" @default.
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