PTP1B mediates the inhibitory effect of MFGE8 on insulin signaling through the β5 integrin.

ABSTRACT: Integrins are cell adhesion receptors that dimerize to mediate cell-cell interactions and regulate processes, including proliferation, inflammation, and tissue repair. The role of integrins in regulating insulin signaling is incompletely understood. We have previously shown that binding of the integrin ligand milk fat globule epidermal growth factor like 8 (MFGE8) to the αvβ5 integrin promotes termination of insulin receptor signaling in mice. Upon ligation of MFGE8, integrin β5 complexes with the insulin receptor beta (IRβ) in skeletal muscle, resulting in dephosphorylation of IRβ and reduction of insulin-stimulated glucose uptake. Here, we investigate the mechanism by which the interaction between β5 and IRβ impacts IRβ phosphorylation status. We show in in vitro and in vivo in skeletal

SUBMITTER: Datta R 

PROVIDER: S-EPMC10850974 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature