Title : Osmotic stress-mediated activation of RET kinases involves intracellular disulfide-bonded dimer formation.

Pub. Date : 2001 Jun

PMID : 11491658






4 Functional Relationships(s)
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1 Osmotic stress-mediated activation of RET kinases involves intracellular disulfide-bonded dimer formation. Disulfides ret proto-oncogene Homo sapiens
2 A few percentage of RET proteins normally formed disulfide-bonded dimers in the cell, and osmotic stress promoted formation of these dimers. Disulfides ret proto-oncogene Homo sapiens
3 Osmotic stress also promoted activation and disulfide-bonded dimerization of the extracellular domain-depleted mutant RET (RET-PTC-1), suggesting that the target amino acid(s) for dimerization is located intracellularly rather than in the cysteine-rich region of the extracellular domain. Disulfides ret proto-oncogene Homo sapiens
4 Osmotic stress also promoted activation and disulfide-bonded dimerization of the extracellular domain-depleted mutant RET (RET-PTC-1), suggesting that the target amino acid(s) for dimerization is located intracellularly rather than in the cysteine-rich region of the extracellular domain. Disulfides ret proto-oncogene Homo sapiens