MET dimers autophosphorylate

Stable Identifier
Reaction [transition]
Homo sapiens
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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
8208547 Autophosphorylation modulates the kinase activity and oncogenic potential of the Met receptor tyrosine kinase

Rodrigues, GA, Park, M

Oncogene 1994
8302603 Tyrosines1234-1235 are critical for activation of the tyrosine kinase encoded by the MET proto-oncogene (HGF receptor)

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

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

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

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

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

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

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

J. Biol. Chem. 1991
Catalyst Activity

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

This event is regulated