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The HER2 (c-erbB-2) gene encodes a protein, p185HER2, which possesses all of the structural characteristics and functional
properties of a growth factor receptor, although its ligand has not yet been well characterized. HER2 is the human homolog
of the rat proto-oncogene neu and is closely related to the gene encoding the epidermal growth factor receptor. Amplification
of this gene and overexpression have been found to be a prognostic criterion for a 30% subpopulation of human breast cancer
patients. In this study, we investigated the role of the transmembrane-spanning sequence in the biosynthesis and localization
of p185HER2. A truncation mutant lacking the cytoplasmic and transmembrane domains was glycosylated and efficiently secreted.
However, a mutant lacking only the transmembrane-spanning sequence was incompletely glycosylated and failed to reach the cell
surface. Unexpectedly, although this deletion mutant was retained in the endoplasmic reticulum membrane, it was still able
to transform NIH 3T3 cells when expressed at high levels.