MET dimers autophosphorylate

Stable Identifier
R-HSA-6806974
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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The activated MET receptor autophosphorylates on four tyrosine residues. Two tyrosines, Y1234 and Y1235 are located in the kinase domain of MET and their phosphorylation increases the catalytic activity of MET. Y1235 is the major phosphorylation site (Ferracini et al. 1991, Longati et al. 1994, Rodrigues and Park 1994). The other two MET tyrosines that undergo autophosphorylation are Y1349 and Y1356. These two tyrosines are at the C-terminus of MET and serve as docking sites for binding of MET effectors (Ponzetto et al. 1994, Weidner et al. 1995). It is uncertain whether tyrosine residue Y1365 is also autophosphorylated.

Literature References
PubMed ID Title Journal Year
8302603 Tyrosines1234-1235 are critical for activation of the tyrosine kinase encoded by the MET proto-oncogene (HGF receptor)

Longati, P, Bardelli, A, Ponzetto, C, Naldini, L, Comoglio, PM

Oncogene 1994
8208547 Autophosphorylation modulates the kinase activity and oncogenic potential of the Met receptor tyrosine kinase

Rodrigues, GA, Park, M

Oncogene 1994
7708691 Mutation of juxtamembrane tyrosine residue 1001 suppresses loss-of-function mutations of the met receptor in epithelial cells

Weidner, KM, Sachs, M, Riethmacher, D, Birchmeier, W

Proc. Natl. Acad. Sci. U.S.A. 1995
7513258 A multifunctional docking site mediates signaling and transformation by the hepatocyte growth factor/scatter factor receptor family

Ponzetto, C, Bardelli, A, Zhen, Z, Maina, F, dalla Zonca, P, Giordano, S, Graziani, A, Panayotou, G, Comoglio, PM

Cell 1994
1655790 Identification of the major autophosphorylation site of the Met/hepatocyte growth factor receptor tyrosine kinase

Ferracini, R, Longati, P, Naldini, L, Vigna, E, Comoglio, PM

J. Biol. Chem. 1991
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
protein tyrosine kinase activity of HGF:MET dimer [plasma membrane]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created