| Autor: |
Chan Wah Hak, L., Khan, S., Di Meglio, I., Law, A.-L., Häsler, S.L.-A., Quintaneiro, L.M., Ferreira, A.P.A., Krause, M., McMahon, H.T., Boucrot, Emmanuel |
| Jazyk: |
angličtina |
| Rok vydání: |
2018 |
| Předmět: |
|
| ISSN: |
1465-7392 |
| Popis: |
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, but several clathrin-independent endocytic routes exist in parallel. One such pathway, fast endophilin-mediated endocytosis (FEME), is not constitutive but triggered upon activation of certain receptors, including the β adrenergic receptor. FEME activates promptly following stimulation as endophilin is pre-enriched by the phosphatidylinositol-3,4-bisphosphate-binding protein lamellipodin. 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. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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