ArticleThe Journal of cell biology1988
Overexpression of epidermal growth factor receptor in NIH-3T3-transfected cells slows its lateral diffusion and rate of endocytosis.
Article in The Journal of cell biology, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 35 citations in OpenAlex.
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- Studies of distribution, location and dynamic properties of EGFR on the cell surface measured by image correlation spectroscopy.European biophysics journal : EBJ · 2008Article
- Computational modeling reveals molecular details of epidermal growth factor binding.BMC cell biology · 2005Article
- Activated K-Ras and H-Ras display different interactions with saturable nonraft sites at the surface of live cells.The Journal of cell biology · 2002Article
- Epidermal growth factor receptor distribution during chemotactic responses.Molecular biology of the cell · 2000Article
- Protein targeting by tyrosine- and di-leucine-based signals: evidence for distinct saturable components.The Journal of cell biology · 1996Article
- Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers.The Journal of cell biology · 1996Article
- Insulin receptors internalize by a rapid, saturable pathway requiring receptor autophosphorylation and an intact juxtamembrane region.The Journal of cell biology · 1991Article
- Kinetics of epidermal growth factor/receptor binding on cells measured by total internal reflection/fluorescence recovery after photobleaching.Journal of fluorescence · 1991Article
- Translational diffusion of class II major histocompatibility complex molecules is constrained by their cytoplasmic domains.The Journal of cell biology · 1989Article
- Characterization of internalization and endosome formation of epidermal growth factor in transfected NIH-3T3 cells by computerized image-intensified three-dimensional fluorescence microscopy.The Journal of cell biology · 1989Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Interactions between membrane proteins are believed to be important for the induction of transmembrane signaling. Endocytosis is one of the responses which is regulated by both intracellular and extracellular signals. To study such interactions, we have measured the lateral mobility and rate of endocytosis of epidermal growth factor receptor in three transfected NIH-3T3 cell lines (HER84, HER22, and HER82) expressing 2 X 10(4), 2 X 10(5) and 1.5 X 10(6) EGF-receptors per cell, respectively. Using rhodamine-labeled EGF (Rh-EGF) and rhodamine-labeled monoclonal anti-EGF-receptor antibody (Rh-mAb-108), we measured twofold decreases in the lateral diffusion coefficients for each approximately 10-fold increase in EGF-receptor concentration. Since steric effects cannot account for such dependence, we propose that protein mobility within the membrane, which is determined by the rate of motion between immobile barriers, decreases due to aggregate formation. The rate of endocytosis also decreases twofold between the HER84 (2 X 10(4) receptors/cell) and HER22 (2 X 10(5) receptors/cell) cell lines, suggesting that it is diffusion limited. The comparable rates of endocytosis of the HER82 and HER22 cell lines suggest that at high receptor density endocytosis may be limited by the total number of sites for receptors in coated-pits and by their rate of recycling.
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