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The carboxyl‐terminal domain of insulin‐like growth factor‐I receptor interacts with the insulin receptor and activates its protein tyrosine kinase
Author(s) -
Li Shu-lian,
Termini John,
Hayward Amanda,
Siddle Ken,
Zick Yehiel,
Koval Anatolii,
LeRoith Derek,
Fujita-Yamaguchi Yoko
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01523-8
Subject(s) - insulin receptor , tyrosine kinase , chemistry , receptor , biochemistry , insulin , receptor tyrosine kinase , tyrosine , insulin like growth factor , grb10 , insulin receptor substrate , microbiology and biotechnology , biophysics , growth factor , biology , endocrinology , insulin resistance
Receptors for insulin and insulin‐like growth factor‐I (IR and IGFIR) consisting of the α 2 β 2 structure are protein tyrosine kinases (PTKs). Carboxyl‐terminal (CT) domains of their β subunits are structurally diverse while the PTK domains share the highest homology. Interactions between CT and PTK domains of IR and IGFIR were studied by means of PTK activity, fluorescence energy transfer or surface plasmon resonance using BIAcore. We present evidence that IGFIR CT directly interacts with both IGFIR and IR. Although binding to both receptors, stimulation of PTK activity only occurs with IR but not IGFIR.