Recycling of epidermal growth factor-receptor complexes in A431 cells: identification of dual pathways

Sorkin, A., Krolenko, S., Kudrjavtceva, N., Lazebnik, J., Teslenko, L., Soderquist, A. M., Nikolsky, N. (1991) Recycling of epidermal growth factor-receptor complexes in A431 cells: identification of dual pathways. Journal of Cell Biology, 112 (1). pp. 55-63. ISSN 0021-9525

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URL: http://www.ncbi.nlm.nih.gov/pubmed/1986007
DOI: 10.1083/jcb.112.1.55

Abstract

The intracellular sorting of EGF-receptor complexes (EGF-RC) has been studied in human epidermoid carcinoma A431 cells. Recycling of EGF was found to occur rapidly after internalization at 37 degrees C. The initial rate of EGF recycling was reduced at 18 degrees C. A significant pool of internalized EGF was incapable of recycling at 18 degrees C but began to recycle when cells were warmed to 37 degrees C. The relative rate of EGF outflow at 37 degrees C from cells exposed to an 18 degrees C temperature block was slower (t1/2 approximately 20 min) than the rate from cells not exposed to a temperature block (t1/2 approximately 5-7 min). These data suggest that there might be both short- and long-time cycles of EGF recycling in A431 cells. Examination of the intracellular EGF-RC dissociation and dynamics of short- and long-time recycling indicated that EGF recycled as EGF-RC. Moreover, EGF receptors that were covalently labeled with a photoactivatable derivative of 125I-EGF recycled via the long-time pathway at a rate similar to that of 125I-EGF. Since EGF-RC degradation was also blocked at 18 degrees C, we propose that sorting to the lysosomal and long-time recycling pathway may occur after a highly temperature-sensitive step, presumably in the late endosomes.

Item Type: Paper
Uncontrolled Keywords: Carcinoma, Squamous Cell Endocytosis Epidermal Growth Factor Humans Iodine Radioisotopes Kinetics Receptor, Epidermal Growth Factor Temperature Tumor Cells, Cultured
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > epidermal growth factor
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
CSHL Authors:
Communities: CSHL labs > Labeznik lab
Depositing User: Matt Covey
Date: 1991
Date Deposited: 12 Dec 2012 17:32
Last Modified: 12 Dec 2012 17:32
PMCID: PMC2288797
Related URLs:
URI: http://repository.cshl.edu/id/eprint/26407

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