ArticleThe Journal of cell biology2011
Clathrin phosphorylation is required for actin recruitment at sites of bacterial adhesion and internalization.
Article in The Journal of cell biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed, 105 citations in OpenAlex.
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- Revisiting Pathogen Exploitation of Clathrin-Independent Endocytosis: Mechanisms and Implications.Cells · 2025Review
- Renal protein reabsorption impairment related to a myxosporean infection in the grass frog (Rana temporaria L.).Parasitology research · 2023Article
- Novel secreted STPKLRR from Vibrio splendidus AJ01 promotes pathogen internalization via mediating tropomodulin phosphorylation dependent cytoskeleton rearrangement.PLoS pathogens · 2023Article
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- Evaluation of the role of clathrin and bacterial viability in the endocytosis ofFrontiers in veterinary science · 2023Article
- Listeria monocytogenes Co-Opts the Host Exocyst Complex To Promote Internalin A-Mediated Entry.Infection and immunity · 2022Article
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- The Ins and Outs of Antigen Uptake in B cells.Frontiers in immunology · 2022Review
- Endophilin A2 regulates B-cell endocytosis and is required for germinal center and humoral responses.EMBO reports · 2021Article
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- Clathrin Light Chains: Not to Be Taken so Lightly.Frontiers in cell and developmental biology · 2021Review
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- Application of advances in endocytosis and membrane trafficking to drug delivery.Advanced drug delivery reviews · 2020Review
- Clathrin light chain A drives selective myosin VI recruitment to clathrin-coated pits under membrane tension.Nature communications · 2019Article
- Enteropathogenic Escherichia coli remodels host endosomes to promote endocytic turnover and breakdown of surface polarity.PLoS pathogens · 2019Article
- Taming the Triskelion: Bacterial Manipulation of Clathrin.Microbiology and molecular biology reviews : MMBR · 2019Review
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
Abstract
Bacterial pathogens recruit clathrin upon interaction with host surface receptors during infection. Here, using three different infection models, we observed that host-pathogen interactions induce tyrosine phosphorylation of clathrin heavy chain. This modification was critical for recruitment of actin at bacteria-host adhesion sites during bacterial internalization or pedestal formation. At the bacterial interface, clathrin assembled to form coated pits of conventional size. Because such structures cannot internalize large particles such as bacteria, we propose that during infection, clathrin-coated pits serve as platforms to initiate actin rearrangements at bacteria-host adhesion sites. We then showed that the clathrin-actin interdependency is initiated by Dab2 and depends on the presence of clathrin light chain and its actin-binding partner Hip1R, and that the fully assembled machinery can recruit Myosin VI. Together, our study highlights a physiological role for clathrin heavy chain phosphorylation and reinforces the increasingly recognized function of clathrin in actin cytoskeletal organization in mammalian cells.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.