eprintid: 1447405 rev_number: 37 eprint_status: archive userid: 608 dir: disk0/01/44/74/05 datestamp: 2014-09-09 18:54:50 lastmod: 2021-09-19 23:44:19 status_changed: 2014-09-09 18:54:50 type: article metadata_visibility: show item_issues_count: 0 creators_name: Grove, J creators_name: Metcalf, DJ creators_name: Knight, AE creators_name: Wavre-Shapton, ST creators_name: Sun, T creators_name: Protonotarios, E creators_name: Griffin, LD creators_name: Lippincott-Schwartz, J creators_name: Marsh, M title: Flat Clathrin Lattices: stable features of the plasma membrane ispublished: pub divisions: UCL divisions: B02 divisions: C08 divisions: D77 divisions: C10 divisions: D15 divisions: B04 divisions: C05 divisions: F48 note: © 2014 Grove et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). abstract: Clathrin-mediated endocytosis (CME) is a fundamental property of eukaryotic cells. Classical CME proceeds via the formation of clathrin-coated pits (CCP) at the plasma membrane that invaginate to form clathrin-coated vesicles; a process that is well understood. However, clathrin also assembles into flat clathrin lattices (FCL); these structures remain poorly described and their contribution to cell biology is unclear. We have used quantitative imaging to provide the first comprehensive description of FCL and explore their influence on plasma membrane organization. Ultrastructural analysis by electron and super-resolution microscopy revealed two discrete populations of clathrin structures. CCP were typified by their sphericity, small size and homogeneity. FCL were planar, large and heterogeneous, and present on both the dorsal and ventral surfaces of cells. Live microscopy demonstrated that CCP are short-lived and culminate in a peak of dynamin recruitment, consistent with classical CME. In contrast, FCL were long-lived with sustained association with dynamin. We investigated the biological relevance of FCL using the chemokine receptor CCR5 as a model system. Agonist activation leads to sustained recruitment of CCR5 to FCL. Quantitative molecular imaging indicated that FCL partitioned receptors at the cell surface. Our observations suggest that FCL provide stable platforms for the recruitment of endocytic cargo. date: 2014-11-05 official_url: http://dx.doi.org/10.1091/mbc.E14-06-1154 vfaculties: VENG oa_status: green full_text_type: pub language: eng primo: open primo_central: open_green article_type_text: JOURNAL ARTICLE verified: verified_manual elements_source: PubMed elements_id: 973043 doi: 10.1091/mbc.E14-06-1154 pii: mbc.E14-06-1154 language_elements: ENG lyricists_name: Griffin, Lewis lyricists_name: Grove, Joseph lyricists_name: Marsh, Mark lyricists_id: LDGRI51 lyricists_id: JGROV82 lyricists_id: MCPMA80 full_text_status: public publication: Mol Biol Cell volume: 25 number: 22 pagerange: 3581 - 3594 issn: 1059-1524 citation: Grove, J; Metcalf, DJ; Knight, AE; Wavre-Shapton, ST; Sun, T; Protonotarios, E; Griffin, LD; ... Marsh, M; + view all <#> Grove, J; Metcalf, DJ; Knight, AE; Wavre-Shapton, ST; Sun, T; Protonotarios, E; Griffin, LD; Lippincott-Schwartz, J; Marsh, M; - view fewer <#> (2014) Flat Clathrin Lattices: stable features of the plasma membrane. Mol Biol Cell , 25 (22) 3581 - 3594. 10.1091/mbc.E14-06-1154 <https://doi.org/10.1091/mbc.E14-06-1154>. Green open access document_url: https://discovery.ucl.ac.uk/id/eprint/1447405/1/Mol._Biol._Cell-2014-Grove-3581-94.pdf