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    The tetrameric adaptor protein AP-3 is critical for the transport of proteins to lysosomes and lysosome-related organelles. The structures of homologous adaptors AP-1 and AP-2 have revealed a closed-to-open conformational change upon membrane recruitment and phosphoinositide binding. Recently, Schoppe et al. reported the first cryo-EM structures of AP-3 from budding yeast and described remarkably flexible solution structures that are all in the open conformation. The apparent lack of a closed conformational state, the first such description in the literature, allows AP-3 to be more reliant on cargo interaction for its initial membrane recruitment compared with AP-1. Copyright © 2021 The Author. Published by Elsevier Inc. All rights reserved.

    Citation

    Todd R Graham. AP-3 shows off its flexibility for the cryo-EM camera. The Journal of biological chemistry. 2022 Jan;298(1):101491

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    PMID: 34902351

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