Antibody-induced dimerization of FGFR1 promotes receptor endocytosis independently of its kinase activity.

ABSTRACT: Fibroblast growth factors (FGFs) and their plasma membrane-localized receptors (FGFRs) play a key role in the regulation of developmental processes and metabolism. Aberrant FGFR signaling is associated with the progression of serious metabolic diseases and human cancer. Binding of FGFs to FGFRs induces receptor dimerization and transphosphorylation of FGFR kinase domains that triggers activation of intracellular signaling pathways. Following activation, FGFRs undergo internalization and subsequent lysosomal degradation, which terminates transmission of signals. Although factors that regulate FGFR endocytosis are continuously discovered, little is known about the molecular mechanism that initiates the internalization of FGFRs. Here, we analyzed the internalization of antibody fragments in v

SUBMITTER: Opalinski L 

PROVIDER: S-EPMC5540934 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature