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    Fbp17 and cip4 recruit ship2 and lamellipodin to prime the plasma membrane for fast endophilin-mediated endocytosis

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    Authors
    Hak, Laura Chan Wah
    Khan, Shaheen
    Meglio, Ilaria Di
    Law, Ah-Lai
    Häsler, Safa Lucken-Ardjomande
    Quintaneiro, Leonor M.
    Ferreira, Antonio P.A.
    Krause, Matthias
    McMahon, Harvey T.
    Boucrot, Emmanuel
    Issue Date
    2018-07-30
    Subjects
    endocytosis
    
    Metadata
    Show full item record
    Abstract
    Endocytosis mediates the cellular uptake of micronutrients and the turnover of plasma membrane proteins. Clathrin-mediated endocytosis is the major uptake pathway in resting cells 1 , but several clathrin-independent endocytic routes exist in parallel 2,3 . One such pathway, fast endophilin-mediated endocytosis (FEME), is not constitutive but triggered upon activation of certain receptors, including the β 1 adrenergic receptor 4 . FEME activates promptly following stimulation as endophilin is pre-enriched by the phosphatidylinositol-3,4-bisphosphate-binding protein lamellipodin 4,5 . However, in the absence of stimulation, endophilin foci abort and disassemble after a few seconds. Looking for additional proteins involved in FEME, we found that 20 out of 65 BAR domain-containing proteins tested colocalized with endophilin spots. Among them, FBP17 and CIP4 prime the membrane of resting cells for FEME by recruiting the 5′-lipid phosphatase SHIP2 and lamellipodin to mediate the local production of phosphati-dylinositol-3,4-bisphosphate and endophilin pre-enrichment. Membrane-bound GTP-loaded Cdc42 recruits FBP17 and CIP4, before being locally deactivated by RICH1 and SH3BP1 GTPase-activating proteins. This generates the transient assembly and disassembly of endophilin spots, which lasts 5–10 seconds. This mechanism periodically primes patches of the membrane for prompt responses upon FEME activation.
    Citation
    Hak LCW, Khan S, Meglio ID, Law AL, Häsler SLA, Quintaneiro LM, Ferreira APA, Krause M, McMahon HT, Boucrot E (2018) 'Fbp17 and cip4 recruit ship2 and lamellipodin to prime the plasma membrane for fast endophilin-mediated endocytosis', Nature Cell Biology, 20 (9), pp.1023-1031.
    Publisher
    Nature Publishing Group
    Journal
    Nature Cell Biology
    URI
    http://hdl.handle.net/10547/624683
    DOI
    10.1038/s41556-018-0146-8
    PubMed ID
    30061681
    PubMed Central ID
    PMC6122583
    Additional Links
    https://www.nature.com/articles/s41556-018-0146-8
    https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6122583/
    Type
    Article
    Language
    en
    ISSN
    1465-7392
    ae974a485f413a2113503eed53cd6c53
    10.1038/s41556-018-0146-8
    Scopus Count
    Collections
    Biomedical and biological science

    entitlement

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    • Publisher Correction: FBP17 and CIP4 recruit SHIP2 and lamellipodin to prime the plasma membrane for fast endophilin-mediated endocytosis.
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