Fbp17 and cip4 recruit ship2 and lamellipodin to prime the plasma membrane for fast endophilin-mediated endocytosis
Authors
Hak, Laura Chan WahKhan, 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
2018-07-30Subjects
endocytosis
Metadata
Show full item recordAbstract
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 GroupJournal
Nature Cell BiologyPubMed ID
30061681PubMed Central ID
PMC6122583Additional Links
https://www.nature.com/articles/s41556-018-0146-8https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6122583/
Type
ArticleLanguage
enISSN
1465-7392ae974a485f413a2113503eed53cd6c53
10.1038/s41556-018-0146-8