The carboxyl-terminal SH3 domain of the mammalian adaptor CrkII promotes internalization of Listeria monocytogenes through activation of host phosphoinositide 3-kinase

    Authors

    H. Dokainish; B. Gavicherla; Y. Shen;K. Ireton

    Comments

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    Abbreviated Journal Title

    Cell Microbiol.

    Keywords

    PHOSPHATIDYLINOSITOL 3-KINASE; TYROSINE-PHOSPHORYLATION; ACTIN; POLYMERIZATION; HELICOBACTER-PYLORI; SIGNALING PATHWAY; EPITHELIAL-CELLS; SURFACE PROTEIN; SMALL GTPASES; INIB PROTEIN; MET; RECEPTOR; Cell Biology; Microbiology

    Abstract

    The intracellular bacterial pathogen Listeria monocytogenes causes food-borne illnesses leading to gastroenteritis, meningitis or abortion. Listeria induces its internalization into some mammalian cells through binding of the bacterial surface protein InlB to its host receptor, the Met Receptor Tyrosine Kinase. InlB-induced activation of Met stimulates host signal transduction pathways that culminate in cell surface changes driving pathogen engulfment. One mammalian protein with the potential to couple Met to downstream signalling is the adaptor CrkII. CrkII contains an unusual carboxyl-terminal SH3 domain (SH3C) that promotes entry of Listeria. However, binding partners or downstream effectors of SH3C remain unknown. Here, we use RNA interference and overexpression studies to demonstrate that SH3C affects bacterial uptake, at least in part, through stimulation of host phosphatidylinositide (PI) 3-kinase. Experiments with latex beads coated with InlB protein indicated that one potential role of SH3C and PI 3 kinase is to promote changes in the F-actin cytoskeleton necessary for particle engulfment. Taken together, our results indicate that the CrkII SH3C domain engages a cellular ligand that regulates PI 3 kinase activity and host cell surface rearrangements.

    Journal Title

    Cellular Microbiology

    Volume

    9

    Issue/Number

    10

    Publication Date

    1-1-2007

    Document Type

    Article

    Language

    English

    First Page

    2497

    Last Page

    2516

    WOS Identifier

    WOS:000249221700016

    ISSN

    1462-5814

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