Clathrin phosphorylation is required for actin recruitment at sites of bacterial adhesion and internalization

Bonazzi, Matteo; Vasudevan, Lavanya; Mallet, Adeline; Sachse, Martin; Sartori, Anna; Prévost, Marie-Claude; Roberts, Allison; Taner, Sabrina B.; Wilbur, Jeremy D.; Brodsky, Frances M.; Cossart, Pascale

doi:10.1083/jcb.201105152

Cited by 102 publications

(147 citation statements)

References 48 publications

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“…The clathrin-mediated endocytosis machinery is involved in the cell invasion by L. monocyto-genes (Veiga and Cossart 2005;Veiga et al 2007;Bonazzi et al 2011). For both the InlA and the InlB pathways, the initial events in the internalization process are the posttranslational modifications of the two main Listeria receptors E-cadherin and Met: Indeed, E-cadherin is phosphorylated by Src and then ubiquitinated by Hakai (Bonazzi et al 2008), whereas Met autophosphorylation leads to the recruitment of Cbl, which in turn ubiquitinates Met (Veiga and Cossart 2005).…”

Section: The Clathrin-mediated Endocytosis Machinery Is Involved In Tmentioning

confidence: 99%

Entry of Listeria monocytogenes in Mammalian Epithelial Cells: An Updated View

Pizarro‐Cerdá

Kühbacher

Cossart

2012

Cold Spring Harbor Perspectives in Medicine

221

202

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Listeria monocytogenes is a bacterial pathogen that promotes its internalization into host epithelial cells. Interaction between the bacterial surface molecules InlA and InlB and their cellular receptors E-cadherin and Met, respectively, triggers the recruitment of endocytic effectors, the subversion of the phosphoinositide metabolism, and the remodeling of the actin cytoskeleton that lead to bacterial engulfment. Additional bacterial surface and secreted virulence factors also contribute to entry, albeit to a lesser extent. Here we review the increasing number of signaling effectors that are reported as being subverted by L. monocytogenes during invasion of cultured cell lines. We also update the current knowledge of the early steps of in vivo cellular infection, which, as shown recently, challenges previous concepts generated from in vitro data.

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Section: The Clathrin-mediated Endocytosis Machinery Is Involved In Tmentioning

confidence: 99%

Entry of Listeria monocytogenes in Mammalian Epithelial Cells: An Updated View

Pizarro‐Cerdá

Kühbacher

Cossart

2012

Cold Spring Harbor Perspectives in Medicine

221

202

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“…Clathrin also mediates entry of large viruses and other bacteria using zipper mechanism [70][71][72] and also pedestal formation by the extracellular enteropathogenic E. coli (EPEC) [72]. Interestingly, by analysing the molecular events during early stages of L. monocytogenes and EPEC infection, it was 14 observed that Myosin VI, a myosin that moves on actin filaments towards the minus ends, accumulates at the L. monocytogenes entry sites but not at the EPEC-induced actin-based pedestals [73]. Knowckdown of Myosin IV inhibits L. monocytogenes entry but does not reduce the recruitment of the clathrin-actin machinery at bacterial adhesion sites, suggesting the Myosin VI is the last component of this machinery and provides the pulling force for bacterial internalisation.…”

Section: A Role For Clathrin and Two Myosins In Bacterial Entrymentioning

confidence: 99%

How the Study of Listeria Monocytogenes has Led to New Concepts in Biology

Rolhion

Cossart

2017

Future Microbiol.

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The opportunistic intracellular bacterial pathogen Listeria monocytogenes has in 30 years emerged as an exceptional bacterial model system in infection biology. Research on this bacterium has provided considerable insight into how pathogenic bacteria adapt to mammalian hosts, invade eukaryotic cells, move intracellularly, interfere with host cell functions and disseminate within tissues. It also contributed to unveil features of normal host cells pathways and unsuspected functions of previously known cellular proteins. This review provides an updated overview of our knowledge on this pathogen. In many examples, findings on Listeria monocytogenes provided the basis for new concepts in bacterial regulation, cell biology and infection processes.

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“…CHC17 phophorylation is induced by the binding of internalin A protein of Listeria to cadherin. These steps organize actin cytoskeleton around CHC17 to internalize cell-bound Listeria (18,19). It is important to point out that this internalization step is uniquely different from conventional clathrin vesicle formation.…”

Section: Clathrin Hip Actin and Infectionmentioning

confidence: 99%

“…Enteropathic Escherichia coli (EPEC) has also developed an infection pathway that takes advantage of CHC17/HIP function. The phosphorylation of CHC17 at the EPEC/host interface induces clathrin-associated actin to form a pedestal structure into the host to import pathogenic molecules from attached EPEC (19).…”

Section: Clathrin Hip Actin and Infectionmentioning

confidence: 99%

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Novel clathrin activity: developments in health and disease

Ybe

2014

Biomolecular Concepts

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Clathrin self-assembles into a coat around vesicles filled with cargo such as nutrients, hormones, and proteins destined for degradation. Recent developments indicate clathrin is not a specialist, but is involved in different processes relevant to health and disease. Clathrin is used to strengthen centrosomes and mitotic spindles essential for chromosome segregation in cell division. In Wnt signaling, clathrin is a component of signalosomes on the plasma membrane needed to produce functional Wnt receptors. In glucose metabolism, a muscle-specific isoform, CHC22 clathrin, is key to the formation of storage compartments for GLUT4 receptor, and CHC22 dysfunction has been tied to type 2 diabetes. The activity of clathrin to self-assemble and to work with huntingtin-interacting proteins to organize actin is exploited by Listeria and enteropathic Escherichia coli in their infection pathways. Finally, there is an important connection between clathrin and human malignancies. Clathrin is argued to help transactivate tumor suppressor p53 that controls specific genes in DNA repair and apoptosis. However, this is debatable because trimeric clathrin must be made monomeric. To get insight on how the clathrin structure could be converted, the crystal structure of the trimerization domain is used in the development of the detrimerization switch hypothesis. This novel hypothesis will be relevant if connections continue to be found between CHC17 and p53 anti-cancer activity in the nucleus.

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Clathrin phosphorylation is required for actin recruitment at sites of bacterial adhesion and internalization

Abstract: Clathrin assembles at bacterial adhesion sites and its phosphorylation is required for actin recruitment during bacterial infection.

Cited by 102 publications

References 48 publications

Entry of Listeria monocytogenes in Mammalian Epithelial Cells: An Updated View

Entry of Listeria monocytogenes in Mammalian Epithelial Cells: An Updated View

How the Study of Listeria Monocytogenes has Led to New Concepts in Biology

Novel clathrin activity: developments in health and disease

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