Format

Send to

Choose Destination
FEBS Lett. 1994 Aug 22;350(2-3):230-4.

Evidence for N-glycosylation and ubiquitination of the prolactin receptor expressed in a baculovirus-insect cell system.

Author information

1
Laboratoire de Pathologie Comparée, Institut National de la Recherche Agronomique, CNRS UA 1184, St-Christol-Lez-Alès, France.

Abstract

The molecular mass of the rabbit prolactin receptor (rbPRLR) deduced from cDNA cloning is 66 kDa. However, the molecular mass of the full-length receptor expressed in the insect Sf9 cells was found to be 94 kDa. In order to explain this discrepancy, we analyzed the possible post-translational modifications of the PRLR. Sf9 cells were infected with recombinant baculoviruses in the presence of tunicamycin, an inhibitor of N-glycosylation. Results showed that an additional approximately 9 kDa of the extracellular domain could be attributed to the N-glycosylation and another additional approximately 20 kDa covalent modification occurred in the cytoplasmic part of the receptor. Western blot analysis, using anti-ubiquitin antibodies, revealed that the rbPRLR was ubiquitinated in its cytoplasmic domain.

PMID:
8070570
DOI:
10.1016/0014-5793(94)00772-1
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center