N-glycosylation of the prolactin receptor is not required for activation of gene transcription but is crucial for its cell surface targeting

Molecular Endocrinology
H ButeauM Edery

Abstract

The functional importance of the three oligosaccharide chains linked to Asn35, Asn80 and Asn108, of the long form of the PRL receptor (PRLR) was investigated by individual or multiple substitutions of asparagyl residues using site-directed mutagenesis and transient transfection of these mutated forms of PRLR in monkey kidney cells, Chinese hamster ovary, and human 293 fibroblast cells that exhibit different levels of protein expression. Scatchard analysis performed on monkey kidney cells revealed that the mutants possess the same affinity for PRL as compared with wild-type PRLR. A strong reduction (90%) of the aglycosylated PRLR expression at the cell surface of monkey kidney or human 293 cells was observed. Immunohistochemistry experiments using an anti-PRLR monoclonal antibody showed an accumulation of the deglycosylated receptor in the Golgi area of transfected monkey kidney cells. Upon PRL stimulation, the aglycosylated PRLR associated with Janus kinase 2 was phosphorylated and was able to activate a beta-casein gene promoter in transfected 293 fibroblast cells. The active form of the PRLR was thus acquired independently of glycosylation. By contrast, no functional activity was detectable in transfected Chinese hamster ovar...Continue Reading

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Citations

Jan 22, 2008·Journal of Mammary Gland Biology and Neoplasia·G SwaminathanS Y Fuchs
May 12, 2012·Endocrine Reviews·Charles L Brooks
Oct 11, 2012·Journal of Molecular Endocrinology·J M FlemingP Goldsmith
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