| Literature DB >> 34155137 |
Nathan M Willy1, Federico Colombo2, Scott Huber1, Anna C Smith2, Erienne G Norton2, Comert Kural3,4, Emanuele Cocucci5,6.
Abstract
The most represented components of clathrin-coated vesicles (CCVs) are clathrin triskelia and the adaptors clathrin assembly lymphoid myeloid leukemia protein (CALM) and the heterotetrameric complex AP2. Investigation of the dynamics of AP180-amino-terminal-homology (ANTH) recruitment during CCV formation has been hampered by CALM toxicity upon overexpression. We used knock-in gene editing to express a C-terminal-attached fluorescent version of CALM, while preserving its endogenous expression levels, and cutting-edge live-cell microscopy approaches to study CALM recruitment at forming CCVs. Our results demonstrate that CALM promotes vesicle completion upon membrane tension increase as a function of the amount of this adaptor present. Since the expression of adaptors, including CALM, differs among cells, our data support a model in which the efficiency of clathrin-mediated endocytosis is tissue specific and explain why CALM is essential during embryogenesis and red blood cell development.Entities:
Keywords: clathrin adaptors; lattice light-sheet microscopy; membrane tension; membrane traffic; quantitative microscopy
Mesh：
Substances：
Year: 2021 PMID： 34155137 PMCID： PMC8237669 DOI： 10.1073/pnas.2010438118
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205