InlB:MET dimer trans-autophophorylates

Stable Identifier
R-HSA-8876230
Type
Reaction [transition]
Species
Homo sapiens
Related Species
Listeria monocytogenes
Compartment
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MET bound to Listeria monocytogenes InlB protein undergoes trans-autophosphorylation. Phosphorylation at tyrosine residues Y1234 and Y1235 in the activation loop of the kinase domain of MET was specifically demonstrated. As InlB-activated MET activates downstream signaling by ERKs (MAPKs) and PI3K/AKT, MET is presumably phosphorylated on GRB2 and GAB1 docking sites Y1349 and Y1356, respectively (Niemann et al. 2007, Ferraris et al. 2010).

Literature References
PubMed ID Title Journal Year
17662939 Structure of the human receptor tyrosine kinase met in complex with the Listeria invasion protein InlB

Niemann, HH, J├Ąger, V, Butler, PJ, van den Heuvel, J, Schmidt, S, Ferraris, D, Gherardi, E, Heinz, DW

Cell 2007
19900460 Ligand-mediated dimerization of the Met receptor tyrosine kinase by the bacterial invasion protein InlB

Ferraris, DM, Gherardi, E, Di, Y, Heinz, DW, Niemann, HH

J. Mol. Biol. 2010
Participants
Participates
Catalyst Activity

protein tyrosine kinase activity of InlB:MET dimer [plasma membrane]

Disease
Name Identifier Synonyms
listeriosis DOID:11573 Infection by Listeria monocytogenes, Infection due to Listeria monocytogenes, Listeria infection, Listeriosis
Authored
Reviewed
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