Activation of receptor protein-tyrosine kinases from the cytoplasmic compartment

• Published in: Journal of biochemistry (Tokyo) Vol. 151; no. 4; pp. 353 - 359
• Main Authors: Yamanashi, Yuji, Tezuka, Tohru, Yokoyama, Kazumasa
• Format: Journal Article
• Language: English
• Published: England 01.04.2012
• Subjects: Animals; Cytoplasm - enzymology; Cytoplasm - metabolism; Enzyme Activation; Guanine Nucleotide Exchange Factors - metabolism; Humans; Molecular Targeted Therapy; Muscle Proteins - genetics; Muscle Proteins - metabolism; Myasthenia Gravis - drug therapy; Myasthenia Gravis - enzymology; Myasthenia Gravis - genetics; Myoblasts - enzymology; Myoblasts - metabolism; Neoplasms - drug therapy; Neoplasms - enzymology; Neuromuscular Junction - enzymology; Neuromuscular Junction - metabolism; Protein Binding; Receptor Protein-Tyrosine Kinases - metabolism

It is widely accepted that receptor protein-tyrosine kinases (RTKs) are activated upon dimerization by binding to their extracellular ligands. However, EGF receptor (EGFR) dimerization per se does not require ligand binding. Instead, its cytoplasmic kinase domains have to form characteristic head-to...