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FBP17 and CIP4 recruit SHIP2 and lamellipodin to prime the plasma membrane for fast endophilin-mediated endocytosis

  • Laura Chan Wah Hak
    ,
  • Shaheen Khan
    ,
  • Ilaria Di Meglio
    ,
  • Ah Lai Law
    ,
  • Safa Lucken Ardjomande Häsler
    ,
  • Leonor M. Quintaneiro
*Corresponding author for this work
  • University College London
    ,
  • University of Oxford
    ,
  • University of Geneva
    ,
  • King's College London
    ,
  • Medical Research Council
    ,
  • Harvard University
Research Output:
Contribution to journal
Letter
 Peer-review

Open access

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.

Publication Information

Output type

Research Output:
Contribution to journal
Letter
 Peer-review

Original language

English

Pages from-to (Number of pages)

Pages 1023-1031

Journal (Volume, Issue Number)

Nature Cell Biology (Volume 20, Issue 9)

Publication milestones

  • Accepted/In press - 20/06/2018
  • Published - 30/07/2018

Publication status

Published - 30/07/2018

ISSN

1465-7392

Publication IDs

  • handle.net: 10547/624683
  • Scopus: 85052551738
  • PubMed: 30061681

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