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dc.contributor.authorHak, Laura Chan Wah
dc.contributor.authorKhan, Shaheen
dc.contributor.authorMeglio, Ilaria Di
dc.contributor.authorLaw, Ah-Lai
dc.contributor.authorHäsler, Safa Lucken-Ardjomande
dc.contributor.authorQuintaneiro, Leonor M.
dc.contributor.authorFerreira, Antonio P.A.
dc.contributor.authorKrause, Matthias
dc.contributor.authorMcMahon, Harvey T.
dc.contributor.authorBoucrot, Emmanuel
dc.contributor.illustrator
dc.date.accessioned2020-11-26T13:31:56Z
dc.date.available2020-11-26T13:31:56Z
dc.date.issued2018-07-30
dc.identifier.citationHak 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.en_US
dc.identifier.issn1465-7392
dc.identifier.pmid30061681
dc.identifier.doi10.1038/s41556-018-0146-8
dc.identifier.urihttp://hdl.handle.net/10547/624683
dc.description.abstractEndocytosis 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.en_US
dc.language.isoenen_US
dc.publisherNature Publishing Groupen_US
dc.relation.urlhttps://www.nature.com/articles/s41556-018-0146-8en_US
dc.relation.urlhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6122583/en_US
dc.rightsYellow - can archive pre-print (ie pre-refereeing)
dc.subjectendocytosisen_US
dc.titleFbp17 and cip4 recruit ship2 and lamellipodin to prime the plasma membrane for fast endophilin-mediated endocytosisen_US
dc.typeArticleen_US
dc.identifier.journalNature Cell Biologyen_US
dc.identifier.pmcidPMC6122583
dc.date.updated2020-11-26T13:09:52Z
dc.description.notefree to read on PMC but cannot upload to repository


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