Listeria monocytogenes: a multifaceted model

Hamon, Mélanie; Bierne, Hélène; Cossart, Pascale

doi:10.1038/nrmicro1413

Cited by 525 publications

(480 citation statements)

References 113 publications

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“…Indeed, such manubria can be generally regarded as single but large adhering junctions, occupying cell surface areas up to 100 μm 2 ; hence, the total cell-cell adhesive surface can exceed 10 3 μm 2 . Clearly, these interdigitating batterylike arrays of manubria profoundly differ from the much shorter E-cadherin-based cell processes, sparsely set with puncta adhaerentia, as described in the filopodial "zippers" of keratinocyte cultures (Vasioukhin et al 2000) and from the E-cadherin-based tight-fitting cell-to-cell structures of spreading Listeria monocytogenes (Cossart and Lecuit 1998;Hamon et al 2006).…”

Section: Discussionmentioning

confidence: 99%

Processus and recessus adhaerentes: giant adherens cell junction systems connect and attract human mesenchymal stem cells

et al. 2007

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Substrate-adherent cultured cells derived from human bone marrow or umbilical cord blood ("mesenchymal stem cells") are of special interest for regenerative medicine. We report that such cells, which can display considerable heterogeneity with respect to their cytoskeletal protein complement, are often interconnected by special tentacle-like cell processes contacting one or several other cells. These processus adhaerentes, studded with many (usually small) puncta adhaerentia and varying greatly in length (up to more than 400 μm long), either contact each other in the intercellular space ("ET touches") or insert in a tight-fitting manner into deep plasma membrane invaginations (recessus adhaerentes), thus forming a novel kind of long (up to 50 μm) continuous cuff-like junction (manubria adhaerentia). The cell processes contain an actin microfilament core that is stabilized with ezrin, α-actinin, and myosin and accompanied by microtubules, and their adhering junctions are characterized by a molecular complement comprising the transmembrane glycoproteins N-cadherin and cadherin-11, in combination with the cytoplasmic plaque proteins α-and β-catenin, together with p120 ctn , plakoglobin, and afadin. The processes are also highly dynamic and rapidly foreshorten as cell colonies approach a denser state of cell packing. These structures are obviously able to establish cell-cell connections, even over long distances, and can form deep-rooted and tight cell-cell adhesions. The possible relationship to similar cell processes in the embryonic primary mesenchyme and their potential in cell sorting and tissue formation processes in the body are discussed.

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Section: Discussionmentioning

confidence: 99%

Processus and recessus adhaerentes: giant adherens cell junction systems connect and attract human mesenchymal stem cells

et al. 2007

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“…SEPT11 Inactivation Increases Listeria Invasion-Listeria invasion of non-phagocytic cells relies upon the polymerization and depolymerization of actin (13,28) in concert also with the function of SEPT2 (15). To assess the functional consequence of SEPT11 depletion on Listeria invasion, we employed the classic gentamicin survival assay (16).…”

Section: Sept9 and Sept11 Have Non-overlapping Roles In Filamentmentioning

confidence: 99%

“…Because other septins homologous to SEPT11 might compensate for its deficiency (12), the degree to which SEPT11 is required for septin filament structure and function is not yet known. Listeria monocytogenes is an invasive bacterium that enters into most mammalian cells in vitro through the interaction of the bacterial surface protein InlB with its host cellular receptor Met, the hepatocyte growth factor receptor (13). We originally identified SEPT9 associated with phagosomes containing latex beads coated with InlB (14).…”

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confidence: 99%

Septin 11 Restricts InlB-mediated Invasion by Listeria

Mostowy

Danckært

Tham

et al. 2009

Journal of Biological Chemistry

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Septins are filament-forming GTPases implicated in several cellular functions, including cytokinesis. We previously showed that SEPT2, SEPT9, and SEPT11 colocalize with several bacteria entering into mammalian non-phagocytic cells, and SEPT2 was identified as essential for this process. Here, we investigated the function of SEPT11, an interacting partner of SEPT9 whose function is still poorly understood. In uninfected HeLa cells, SEPT11 depletion by siRNA increased cell size but surprisingly did not affect actin filament formation or the colocalization of SEPT9 with actin filaments. SEPT11 depletion increased Listeria invasion, and incubating SEPT11-depleted cells with beads coated with the Listeria surface protein InlB also led to increased entry as compared with control cells. Strikingly, as shown by fluorescence resonance energy transfer, the InlB-mediated stimulation of Met signaling remained intact in SEPT11-depleted cells. Taken together, our results show that SEPT11 is not required for the bacterial entry process and rather restricts its efficacy. Because SEPT2 is essential for the InlB-mediated entry of Listeria, but SEPT11 is not, our findings distinguish the roles of different mammalian septins.Septins were discovered in the budding yeast Saccharomyces cerevisiae (1) where they organize into a ring at the mother-bud neck during cell division (2). Septins are GTPases of 30 -65 kDa found in most eukaryotes, except plants, sharing an essential role in cytokinesis (3, 4). Fourteen septins have been identified in humans and classified on the basis of sequence identity into four distinct groups (3, 5). Septins from different groups polymerize into hetero-oligomeric protein complexes and filaments and may associate with cellular membranes, actin filaments, and microtubules (6, 7). Septins are increasingly regarded as novel cytoskeletal elements (8), but their role in post-mitotic events remains poorly understood.The crystal structure of the SEPT2-SEPT6-SEPT7 complex recently highlighted that septins, as opposed to actin and microtubules, form non-polar filaments (9). In the SEPT7-SEPT6-SEPT2-SEPT2-SEPT6-SEPT7 complex, SEPT2 has a central role in filament formation (9), whereas SEPT6 is thought to be replaceable with other SEPT6 group members, including SEPT11 (3). Widely expressed in mammalian tissues (10), SEPT11 may also be a substitute for SEPT6 in other mammalian septin complexes such as SEPT7-SEPT9-SEPT11 (10) or SEPT5-SEPT7-SEPT11 (11). Because other septins homologous to SEPT11 might compensate for its deficiency (12), the degree to which SEPT11 is required for septin filament structure and function is not yet known. Listeria monocytogenes is an invasive bacterium that enters into most mammalian cells in vitro through the interaction of the bacterial surface protein InlB with its host cellular receptor Met, the hepatocyte growth factor receptor (13). We originally identified SEPT9 associated with phagosomes containing latex beads coated with InlB (14). Given the association of septins with the cytoske...

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“…For example, the receptor-activated signaling pathways that lead to actin polymerization during bacterial infection, similarly to those occurring at the IS, involve Arp2/3, N-WASP, WAVE, CD2AP (CD2-associated protein) and dynamin-2, among other proteins (Hamon et al, 2006;Veiga and Cossart, 2005). Interestingly, it has been recently demonstrated that clathrin, which is well known for its central role in endocytic processes, has a determining role in actin remodelling during bacterial and fungal infections (Veiga and Cossart, 2005;Veiga et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

Endosomal clathrin drives actin accumulation at the immunological synapse

Calabia-Linares

Robles‐Valero

Fuente

et al. 2011

Journal of Cell Science

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SummaryAntigen-specific cognate interaction of T lymphocytes with antigen-presenting cells (APCs) drives major morphological and functional changes in T cells, including actin rearrangements at the immune synapse (IS) formed at the cell-cell contact area. Here we show, using cell lines as well as primary cells, that clathrin, a protein involved in endocytic processes, drives actin accumulation at the IS. Clathrin is recruited towards the IS with parallel kinetics to that of actin. Knockdown of clathrin prevents accumulation of actin and proteins involved in actin polymerization, such as dynamin-2, the Arp2/3 complex and CD2AP at the IS. The clathrin pool involved in actin accumulation at the IS is linked to multivesicular bodies that polarize to the cell-cell contact zone, but not to plasma membrane or Golgi complex. These data underscore the role of clathrin as a platform for the recruitment of proteins that promote actin polymerization at the interface of T cells and APCs.

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Listeria monocytogenes: a multifaceted model

Cited by 525 publications

References 113 publications

Processus and recessus adhaerentes: giant adherens cell junction systems connect and attract human mesenchymal stem cells

Processus and recessus adhaerentes: giant adherens cell junction systems connect and attract human mesenchymal stem cells

Septin 11 Restricts InlB-mediated Invasion by Listeria

Endosomal clathrin drives actin accumulation at the immunological synapse

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