Journal
EUROPEAN JOURNAL OF CELL BIOLOGY
Volume 90, Issue 11, Pages 972-981Publisher
ELSEVIER GMBH, URBAN & FISCHER VERLAG
DOI: 10.1016/j.ejcb.2010.11.014
Keywords
Bacterial pathogenesis; Hepatocyte growth factor; InIB; Internalin; Met; Protein structure; Receptor tyrosine kinase; Signal transduction; Transmembrane signaling
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Funding
- Deutsche Forschungsgemeinschaft [1150]
- Fonds der Chemischen Industrie
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The receptor tyrosine kinase Met plays a pivotal role in vertebrate development and tissue regeneration, its deregulation contributes to cancer. Met is also targeted during the infection by the facultative intracellular bacterium Listeria monocytogenes. The mechanistic basis for Met activation by its natural ligand hepatocyte growth factor/scatter factor (HGF/SF) is only beginning to be understood at a structural level. Crystal structures of Met in complex with L. monocytogenes InIB suggest that Met dimerization by this bacterial invasion protein is mediated by a dimer contact of the ligand. Here, I review the structural basis of Met activation by InIB and highlight parallels and differences to the physiological Met ligand HGF/SF and its splice variant NK1. (C) 2010 Elsevier GmbH. All rights reserved.
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