A mutated transferrin receptor lacking asparagine-linked glycosylation sites shows reduced functionality and an association with binding immunoglobulin protein

Anthony M. Williams, Caroline Enns

Research output: Contribution to journalArticle

52 Citations (Scopus)

Abstract

The function of the transferrin receptor is to transport iron-bound transferrin into the cell. In order to function properly, this dimeric glycoprotein must be expressed on the cell surface and be able to bind transferrin. Site-directed mutagenesis was performed to abolish the three asparagine-linked glycosylation consensus sequences of the human transferrin receptor. The DNA encoding the mutated transferrin receptor was stably transfected into mouse fibroblasts. This form of the human transferrin receptor shows reduced transferrin binding, reduced intersubunit bond formation, and reduced cell surface expression, indicating that the transferrin receptor which lacks asparaginelinked glycosylation is not fully functional. In addition, the mutated form of the receptor is not processed as quickly. It shows an association with an endoplasmic reticular chaperone protein, binding immunoglobulin protein, leading to the hypothesis that the mutated transferrin receptor experiences increased retention in the endoplasmic reticulum.

Original languageEnglish (US)
Pages (from-to)17648-17654
Number of pages7
JournalJournal of Biological Chemistry
Volume266
Issue number26
StatePublished - Sep 15 1991

Fingerprint

Glycosylation
Transferrin Receptors
Asparagine
Immunoglobulins
Carrier Proteins
Association reactions
Transferrin
Mutagenesis
Consensus Sequence
Fibroblasts
Site-Directed Mutagenesis
Protein Binding
Endoplasmic Reticulum
Glycoproteins
Iron
DNA

ASJC Scopus subject areas

  • Biochemistry

Cite this

@article{50bb02dbd226412abfda3a085a12d961,
title = "A mutated transferrin receptor lacking asparagine-linked glycosylation sites shows reduced functionality and an association with binding immunoglobulin protein",
abstract = "The function of the transferrin receptor is to transport iron-bound transferrin into the cell. In order to function properly, this dimeric glycoprotein must be expressed on the cell surface and be able to bind transferrin. Site-directed mutagenesis was performed to abolish the three asparagine-linked glycosylation consensus sequences of the human transferrin receptor. The DNA encoding the mutated transferrin receptor was stably transfected into mouse fibroblasts. This form of the human transferrin receptor shows reduced transferrin binding, reduced intersubunit bond formation, and reduced cell surface expression, indicating that the transferrin receptor which lacks asparaginelinked glycosylation is not fully functional. In addition, the mutated form of the receptor is not processed as quickly. It shows an association with an endoplasmic reticular chaperone protein, binding immunoglobulin protein, leading to the hypothesis that the mutated transferrin receptor experiences increased retention in the endoplasmic reticulum.",
author = "Williams, {Anthony M.} and Caroline Enns",
year = "1991",
month = "9",
day = "15",
language = "English (US)",
volume = "266",
pages = "17648--17654",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "26",

}

TY - JOUR

T1 - A mutated transferrin receptor lacking asparagine-linked glycosylation sites shows reduced functionality and an association with binding immunoglobulin protein

AU - Williams, Anthony M.

AU - Enns, Caroline

PY - 1991/9/15

Y1 - 1991/9/15

N2 - The function of the transferrin receptor is to transport iron-bound transferrin into the cell. In order to function properly, this dimeric glycoprotein must be expressed on the cell surface and be able to bind transferrin. Site-directed mutagenesis was performed to abolish the three asparagine-linked glycosylation consensus sequences of the human transferrin receptor. The DNA encoding the mutated transferrin receptor was stably transfected into mouse fibroblasts. This form of the human transferrin receptor shows reduced transferrin binding, reduced intersubunit bond formation, and reduced cell surface expression, indicating that the transferrin receptor which lacks asparaginelinked glycosylation is not fully functional. In addition, the mutated form of the receptor is not processed as quickly. It shows an association with an endoplasmic reticular chaperone protein, binding immunoglobulin protein, leading to the hypothesis that the mutated transferrin receptor experiences increased retention in the endoplasmic reticulum.

AB - The function of the transferrin receptor is to transport iron-bound transferrin into the cell. In order to function properly, this dimeric glycoprotein must be expressed on the cell surface and be able to bind transferrin. Site-directed mutagenesis was performed to abolish the three asparagine-linked glycosylation consensus sequences of the human transferrin receptor. The DNA encoding the mutated transferrin receptor was stably transfected into mouse fibroblasts. This form of the human transferrin receptor shows reduced transferrin binding, reduced intersubunit bond formation, and reduced cell surface expression, indicating that the transferrin receptor which lacks asparaginelinked glycosylation is not fully functional. In addition, the mutated form of the receptor is not processed as quickly. It shows an association with an endoplasmic reticular chaperone protein, binding immunoglobulin protein, leading to the hypothesis that the mutated transferrin receptor experiences increased retention in the endoplasmic reticulum.

UR - http://www.scopus.com/inward/record.url?scp=0026014164&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026014164&partnerID=8YFLogxK

M3 - Article

C2 - 1894645

AN - SCOPUS:0026014164

VL - 266

SP - 17648

EP - 17654

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 26

ER -