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


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 cells1, but several clathrin-independent endocytic routes exist in parallel2,3. One such pathway, fast endophilin-mediated endocytosis (FEME), is not constitutive but triggered upon activation of certain receptors, including the ?1 adrenergic receptor4. FEME activates promptly following stimulation as endophilin is pre-enriched by the phosphatidylinositol-3,4-bisphosphate-binding protein lamellipodin4,5. 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 phosphatidylinositol-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.

SUBMITTER: Chan Wah Hak L 

PROVIDER: S-EPMC6122583 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature

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

Chan Wah Hak Laura L   Khan Shaheen S   Di Meglio Ilaria I   Law Ah-Lai AL   Lucken-Ardjomande Häsler Safa S   Quintaneiro Leonor M LM   Ferreira Antonio P A APA   Krause Matthias M   McMahon Harvey T HT   Boucrot Emmanuel E  

Nature cell biology 20180730 9


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<sup>1</sup>, but several clathrin-independent endocytic routes exist in parallel<sup>2,3</sup>. One such pathway, fast endophilin-mediated endocytosis (FEME), is not constitutive but triggered upon activation of certain receptors, including the β<sub>1</sub> adrenergic receptor<sup>4</sup>. FEME activates promptly foll  ...[more]

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