2000
DOI: 10.1042/bj3470771
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Mutational analysis of the N-linked glycosylation sites of the human insulin receptor

Abstract: Site-directed mutagenesis has been used to remove 15 of the 18 potential N-linked glycosylation sites, in 16 combinations, from the human exon 11-minus receptor isoform. The three glycosylation sites not mutated were asparagine residues 25, 397 and 894, which are known to be important in receptor biosynthesis or function. The effects of these mutations on proreceptor processing into α and β subunits, cell-surface expression, insulin binding and receptor autophosphorylation were assessed in Chinese hamster ovar… Show more

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Cited by 39 publications
(23 citation statements)
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“…However, this affinity is considerably lower than that typically found with the full-length holoreceptor (hIR) (18,(21)(22)(23). In addition to its high affinity for insulin, hIR exhibits nonclassical receptor binding properties suggestive of negative cooperativity or site-site interactions between the two receptor halves, namely accelerated dissociation of labeled insulin in the presence of unlabeled insulin and curvilinear Scatchard plots (24).…”
mentioning
confidence: 79%
“…However, this affinity is considerably lower than that typically found with the full-length holoreceptor (hIR) (18,(21)(22)(23). In addition to its high affinity for insulin, hIR exhibits nonclassical receptor binding properties suggestive of negative cooperativity or site-site interactions between the two receptor halves, namely accelerated dissociation of labeled insulin in the presence of unlabeled insulin and curvilinear Scatchard plots (24).…”
mentioning
confidence: 79%
“…N-Glycosylation of TrkA (34), insulin receptor (35), and epidermal growth factor receptor (36) suppresses ligandindependent activation of these RTKs. In TrkA, even partial deglycosylation is sufficient to cause ligand-independent TrkA phosphorylation, resulting in the recruitment of Shc and phospholipase C-␥ (34).…”
Section: Discussionmentioning
confidence: 99%
“…IR precursor undergoes cotranslational glycosylation, intrachain disulfide-bond formation/isomerization (rearrangement), and disulfidelinked homodimerization at the endoplasmic reticulum (ER). The homodimeric IR precursor is proteolytically processed at the trans-Golgi network (TGN) into the disulfide-linked ␣ 2 ␤ 2 complex, which is transported to plasma membrane via as yet unidentified mechanisms (Ronnett et al, 1984;Arakaki et al, 1987;Olson et al, 1988;Caro et al, 1994;Cheatham and Kahn, 1995;Bass et al, 1998;Elleman et al, 2000).…”
mentioning
confidence: 99%