Studying N-linked glycosylation of receptor tyrosine kinases

Harri M Itkonen, Ian G Mills

Research output: Chapter in Book/Report/Conference proceedingChapter (peer-reviewed)

1 Citation (Scopus)

Abstract

Metabolic alterations have been identified as a frequent event in cancer. This is often associated with increased flux through glycolysis, and also a secondary pathway to glycolysis, hexosamine biosynthetic pathway (HBP). HBP provides substrate for N-linked glycosylation, which occurs in the endoplasmic reticulum and the Golgi apparatus. N-linked glycosylation supports protein folding and correct sorting of proteins to plasma membrane and secretion. This process generates complex glycoforms, which can be recognized by other proteins and glycosylation of receptor tyrosine kinases (RTK) can also regulate their plasma-membrane retention time. Of special interest for experimental biologists, plants produce proteins, termed lectins, which bind with high specificity to glyco-conjugates. For the purposes of molecular biology, plant lectins can be conjugated to different moieties, such as agarose beads, which enable precipitation of specifically glycosylated proteins. In this chapter, we describe in detail how to perform pull-down experiments with commercially available lectins to identify changes in the glycosylation of RTKs.

Original languageEnglish
Title of host publicationReceptor Tyrosine Kinases: Methods and Protocols Part III
EditorsSerena Germano
Place of PublicationNew York
PublisherSpringer
Pages103-9
Number of pages7
Volume1233
ISBN (Electronic)9781493917891
ISBN (Print)9781493917884
DOIs
Publication statusPublished - 01 Oct 2014

Publication series

NameMethods in Molecular Biology
PublisherSpringer
Volume1233
ISSN (Print)1064-3745

Bibliographical note

© 2015

Keywords

  • Androgens
  • Binding Sites
  • Blotting, Western
  • Cell Line, Tumor
  • Cell Membrane
  • Electrophoresis, Polyacrylamide Gel
  • Endoplasmic Reticulum
  • Gene Expression
  • Glycosylation
  • Golgi Apparatus
  • Humans
  • Male
  • Phytohemagglutinins
  • Prostate
  • Protein Binding
  • Protein Processing, Post-Translational
  • Protein Transport
  • Receptor, IGF Type 1

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