Reactome | MET dimers autophosphorylate

MET dimers autophosphorylate

Stable Identifier

R-HSA-6806974

Type

Reaction [transition]

Species

Homo sapiens

Compartment

plasma membrane, cytosol

ReviewStatus

5/5

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