Ligand-independent dimerization and activation of the oncogenic Xmrk receptor by two mutations in the extracellular domain.

doi:10.1074/jbc.M006574200

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Article

Ligand-independent dimerization and activation of the oncogenic Xmrk receptor by two mutations in the extracellular domain.

The Journal of biological chemistry - 2 Feb 2001

Gómez A, Wellbrock C, Gutbrod H, Dimitrijevic N, Schartl M

Abstract excerpt

Overexpression of the oncogenic receptor tyrosine kinase ONC-Xmrk is the first step in the development of hereditary malignant melanoma in the fish Xiphophorus. However, overexpression of its proto-oncogene counterpart (INV-Xmrk) is not sufficient for the oncogenic function of the receptor. Compared with INV-Xmrk, the ONC-Xmrk receptor displays 14 amino acid changes, suggesting the presence of activating...

Topics

Amino Acid Substitution
Animals
Cells, Cultured
Cyprinodontiformes
Cysteine
Dimerization
Fish Proteins
Glycosylation
Humans
Ligands
Mutation
Oncogenes
Protein Structure, Tertiary
Proto-Oncogene Mas
Receptor Protein-Tyrosine Kinases
Serine
Species Specificity

Source

Open in PubMed

Identifiers

PMID: 11038352
DOI: 10.1074/jbc.M006574200

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