Host adaptor proteins Gab1 and CrkII promote InlB‐dependent entry of Listeria monocytogenes

• Published in: Cellular microbiology Vol. 7; no. 3; pp. 443 - 457
• Main Authors: Sun, Hong, Shen, Yang, Dokainish, Hatem, Holgado‐Madruga, Marina, Wong, Albert, Ireton, Keith
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Science Ltd 01.03.2005
• Subjects: Animals; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Bacterial Proteins - physiology; Cercopithecus aethiops; Intracellular Signaling Peptides and Proteins - metabolism; Listeria monocytogenes; Listeria monocytogenes - pathogenicity; Listeria monocytogenes - physiology; Mutation; Phosphatidylinositol 3-Kinases - metabolism; Phosphorylation; Protein Binding; Protein Tyrosine Phosphatase, Non-Receptor Type 11; Protein Tyrosine Phosphatases - metabolism; Proto-Oncogene Proteins - genetics; Proto-Oncogene Proteins - metabolism; Proto-Oncogene Proteins - physiology; Proto-Oncogene Proteins c-crk; SH2 Domain-Containing Protein Tyrosine Phosphatases; Signal Transduction; src Homology Domains; Vero Cells
• ISSN: 1462-5814; 1462-5822
• DOI: 10.1111/j.1462-5822.2004.00475.x

Summary The bacterial surface protein InlB mediates internalization of Listeria monocytogenes into mammalian cells through interaction with the host receptor tyrosine kinase, Met. InlB/Met interaction results in activation of the host phosphoinositide (PI) 3‐kinase p85‐p110, an event required for ba...