Bita Sehat

TL;DR: IGF-1 promotes the modification of IGF-1R by small ubiquitin-like modifier protein–1 (SUMO-1) and its translocation to the nucleus, demonstrating a SUMOylation-mediated mechanism of IGF -1R signaling that has potential implications for gene regulation.

TL;DR: Evidence is provided that β-arrestin, otherwise known to be involved in the regulation of G protein-coupled receptors, serves as an adaptor to bring the oncoprotein E3 ubiquitin ligase MDM2 to the IGF-1R, which acts as a crucial component in the ubiquitination and down-regulation of the receptor.

TL;DR: It is demonstrated that IGF-1R stimulation also leads to ubiquitination of β-arrestin1, which regulates vesicular trafficking and activation of ERK1/2, which suggests that β-Arrestin-dependent ERK signaling by the IGF- 1R regulates cell cycle progression and may be an important regulator of the growth of normal and malignant cells.

TL;DR: Results show that c-Cbl constitutes a new ligase responsible for the ubiquitination of IGF-IR and that it complements the action of Mdm2 on ubiquitin lysine residue specificity, responsiveness to IGF-I, and type of endocytic pathway used.

TL;DR: It is shown that nuclear IGF1R associates with the transcription factor LEF1 and increases promoter activity of LEF 1 downstream target genes cyclin D1 and axin2, suggesting a novel function for IGF1r.