InlB-Dependent Internalization of Listeria Is Mediated by the Met Receptor Tyrosine Kinase

Shen, Yang; Naujokas, Monica A.; Park, Morag; Ireton, Keith

doi:10.1016/s0092-8674(00)00141-0

Cited by 489 publications

(561 citation statements)

References 32 publications

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“…79 The receptor tyrosine kinase Met, the physiological receptor for the hepatocyte growth factor (HGF), was also identified as a host cell receptor for InlB. 80 Through its GW modules, soluble InlB binds directly to cellular GAGs. activation of PrfA, the main transcriptional activator of Listeria spp virulence genes (see regulation section).…”

Section: O N O T D I S T R I B U T Ementioning

confidence: 99%

The arsenal of virulence factors deployed byListeria monocytogenesto promote its cell infection cycle

et al. 2011

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Section: O N O T D I S T R I B U T Ementioning

confidence: 99%

The arsenal of virulence factors deployed byListeria monocytogenesto promote its cell infection cycle

et al. 2011

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“…Taken together, these results definitively establish that SEPT11-depleted HeLa cells are competent to internalize Listeria and 1-m InlB beads. (32). Given the positive impact of SEPT11 depletion on particle entry, we hypothesized that signaling events induced upon InlB-Met interaction could be increased upon SEPT11 depletion.…”

Section: Sept11 Inactivation Increases the Entry Of Inlb-coatedmentioning

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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“…In addition to HGF/SF, Met is the major host receptor for the InlB protein of Listeria monocytogenes (Shen et al, 2000). Entry of L. monocytogenes into epithelial cells, endothelial cells and hepatocytes is considered to play an important role in its pathogenesis.…”

Section: Met Signal Transductionmentioning

confidence: 99%

“…Stimulation of the Met receptor with HGF/SF induces tyrosine phosphorylation of the receptor, and stimulation with high levels of HGF/SF leads to detectable Met receptor ubiquitination and enhanced degradation (Jeffers et al, 1997b;Kamei et al, 1999;Shen et al, 2000;Abella et al, 2005). The juxtamembrane region of Met contains an additional docking site, Y1003, which acts as a negative regulator of Met biological activity , and that is absent in the Tpr-Met oncogene (Figure 1).…”

Section: Regulation Of Met Downregulation: Consequence For Oncogenic mentioning

confidence: 99%

From Tpr-Met to Met, tumorigenesis and tubes

2007

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The receptor for hepatocyte growth factor (HGF)/scatter factor (SF), Met, controls a program of invasive epithelial growth through the coordination of cell proliferation and survival, cell migration and epithelial morphogenesis. This process is important during embryogenesis and for organ regeneration in the adult. However, when deregulated the HGF/SF-Met signaling axis contributes to tumorigenesis and metastasis. Studies on the oncogenic activation of the Met receptor have shed light on the molecular mechanisms underlying the oncogenic activation of receptor tyrosine kinase (RTKs). More than a decade ago, work on the Met related oncogene, Tpr-Met, revealed the mechanism for activation of RTK-derived oncogenes generated following chromosomal translocation. More recently, studies on the mechanisms of downregulation of the Met RTK highlight a role for loss of downregulation in RTK oncogenic activation.

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InlB-Dependent Internalization of Listeria Is Mediated by the Met Receptor Tyrosine Kinase

Cited by 489 publications

References 32 publications

The arsenal of virulence factors deployed byListeria monocytogenesto promote its cell infection cycle

The arsenal of virulence factors deployed byListeria monocytogenesto promote its cell infection cycle

Septin 11 Restricts InlB-mediated Invasion by Listeria

From Tpr-Met to Met, tumorigenesis and tubes

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