http://purl.uniprot.org/citations/30061681 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/30061681 | http://www.w3.org/2000/01/rdf-schema#comment | "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 β1 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."xsd:string |
http://purl.uniprot.org/citations/30061681 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41556-018-0146-8"xsd:string |
http://purl.uniprot.org/citations/30061681 | http://purl.uniprot.org/core/author | "Khan S."xsd:string |
http://purl.uniprot.org/citations/30061681 | http://purl.uniprot.org/core/author | "Krause M."xsd:string |
http://purl.uniprot.org/citations/30061681 | http://purl.uniprot.org/core/author | "McMahon H.T."xsd:string |
http://purl.uniprot.org/citations/30061681 | http://purl.uniprot.org/core/author | "Boucrot E."xsd:string |
http://purl.uniprot.org/citations/30061681 | http://purl.uniprot.org/core/author | "Law A.L."xsd:string |
http://purl.uniprot.org/citations/30061681 | http://purl.uniprot.org/core/author | "Chan Wah Hak L."xsd:string |
http://purl.uniprot.org/citations/30061681 | http://purl.uniprot.org/core/author | "Di Meglio I."xsd:string |
http://purl.uniprot.org/citations/30061681 | http://purl.uniprot.org/core/author | "Ferreira A.P.A."xsd:string |
http://purl.uniprot.org/citations/30061681 | http://purl.uniprot.org/core/author | "Lucken-Ardjomande Hasler S."xsd:string |
http://purl.uniprot.org/citations/30061681 | http://purl.uniprot.org/core/author | "Quintaneiro L.M."xsd:string |
http://purl.uniprot.org/citations/30061681 | http://purl.uniprot.org/core/date | "2018"xsd:gYear |
http://purl.uniprot.org/citations/30061681 | http://purl.uniprot.org/core/name | "Nat Cell Biol"xsd:string |
http://purl.uniprot.org/citations/30061681 | http://purl.uniprot.org/core/pages | "1023-1031"xsd:string |
http://purl.uniprot.org/citations/30061681 | http://purl.uniprot.org/core/title | "FBP17 and CIP4 recruit SHIP2 and lamellipodin to prime the plasma membrane for fast endophilin-mediated endocytosis."xsd:string |
http://purl.uniprot.org/citations/30061681 | http://purl.uniprot.org/core/volume | "20"xsd:string |
http://purl.uniprot.org/citations/30061681 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/30061681 |
http://purl.uniprot.org/citations/30061681 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/30061681 |
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