EVIDENCE FOR N-GLYCOSYLATION AND UBIQUITINATION OF THE PROLACTIN RECEPTOR EXPRESSED IN A BACULOVIRUS-INSECT CELL SYSTEM

被引：25

作者：

CAHOREAU, C

GARNIER, L

DJIANE, J

DEVAUCHELLE, G

CERUTTI, M

机构：

[1] INRA, UNITE BIOL CELLULAIRE & MOLEC,PATHOL COMPAREE LAB, CNRS,UA 1184, F-30380 ST CHRISTOL LES ALES, FRANCE

[2] INRA, UNITE ENDOCRINOL MOLEC, F-78352 JOUY EN JOSAS, FRANCE

来源：

FEBS LETTERS | 1994年 / 350卷 / 2-3期

关键词：

BACULOVIRUS; CYTOPLASMIC RECEPTOR DOMAIN; PROLACTIN; N-GLYCOSYLATION; UBIQUITINATION;

D O I：

10.1016/0014-5793(94)00772-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 approximate to 9 kDa of the extracellular domain could be attributed to the N-glycosylation and another additional approximate to 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.

引用

页码：230 / 234

页数：5

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