title: Ectodomain shedding and remnant peptide signalling of EGFRs and their ligands.
abstract: Both receptor tyrosine kinases epidermal growth factor receptors (EGFRs) and their ligands are transmembrane proteins. It has been known that ligand binding activates cytoplasmic tyrosine kinase domains of EGFRs, resulting in the transduction of signals for cell proliferation, migration, differentiation or survival. In an EGFRs-ligands system, however, signal transduction occurs not only unidirectionally but also bidirectionally, which is regulated by cell-cell contact and proteolytic cleavage. Recent studies of proteolytic cleavage 'ectodomain shedding' of EGFRs and their ligands mediated by membrane-type metalloproteinases, a disintegrin and metalloproteinases have been unveiling novel functions and molecular mechanism of their remnant peptides. In addition, the study of the remnant peptide signalling would be essential for understanding the physiological and pathological relevance of anti-shedding therapeutic strategies for diseases such as cancer.
authors: Department of Cell Growth and Tumor Regulation, Proteo-Medicine Research Center (ProMRes), Ehime University, Japan. shigeki@m.ehime-u.ac.jp
authors: Shigeki
authors: S
authors: Higashiyama
authors: Daisuke
authors: D
authors: Nanba
authors: Hironao
authors: H
authors: Nakayama
authors: Hirofumi
authors: H
authors: Inoue
authors: Shinji
authors: S
authors: Fukuda