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The nuclear accumulation of a variant epidermal growth factor receptor (EGFR) lacking the transmembrane domain requires coexpression of a full-length EGFR.
Journal article

The nuclear accumulation of a variant epidermal growth factor receptor (EGFR) lacking the transmembrane domain requires coexpression of a full-length EGFR.

  • Marti U Endocrine and Diabetes Division, Department of Clincal Chemistry, University Hospital, Bern, CH-3010, Switzerland. ulrich.marti@dkf2.unibe.ch
  • Wells A
  • 2000-02-23
Published in:
  • Molecular cell biology research communications : MCBRC. - 2000
3T3 Cells
Alternative Splicing
Animals
Cell Line
Cell Nucleus
Cytoplasm
Enzyme Inhibitors
ErbB Receptors
Genetic Vectors
Humans
Mice
Microscopy, Confocal
Mutagenesis
Mycophenolic Acid
Protein Isoforms
Protein Structure, Tertiary
Transfection
English Both the epidermal growth factor (EGF) and its receptor (EGFR) accumulate in the nucleoplasm during liver regeneration. This localization in a nonmembraneous compartment presents a challenge in that the standard form of EGFR is a transmembrane protein and suggests the existence of a variant, soluble form of EGFR. To investigate the localization of such a putative EGFR splice variant, we generated a transmembrane-devoid form of EGFR. We placed this transmembrane-negative [TM(-)] EGFR construct and full-length wild-type (wt) EGFR either in a retroviral transfection vector or in an inducible expression vector. Mouse 3T3 cells, which express endogenous EGFR, were transfected with the TM(-) EGFR construct. The expression of these TM(-) EGFR, detected with a specific antibody against human EGFR using a confocal laser-scanning microscope, was predominantly found in the cytoplasm with no nuclear localization. After an overnight incubation with EGF the TM(-) EGFR accumulated in the nucleus. In mouse NR6 cells, which lack endogenous EGFR, transfected TM(-) EGFR were found in the cytoplasm, but incubation with EGF did not result in a nuclear accumulation of TM(-) EGFR. However, NR6 cells transfected with both TM(-) EGFR and wt EGFR showed nuclear accumulation after EGF treatment. These results suggest that both the wt EGFR and the TM(-) EGFR are required for nuclear accumulation of TM(-) EGFR and may implicate a model of homotypic recognition and translocation of a splice variant of EGFR.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.rero.ch/global/documents/63881
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