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Proceedings Paper

Rotational diffusion of receptors for epidermal growth factor measured by time-resolved phosphorescence depolarization
Author(s): Raphael Zidovetzki; David Allen Johnson; Donna J. Arndt-Jovin; Thomas M. Jovin
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Paper Abstract

The cell surface receptor for epidermal growth factor (EGFR) is one of the most studied integral membrane proteins. The receptor is widely distributed in cells and tissues of mammalian and avian tissues and plays an important role in growth control. Binding of the epidermal growth factor (EGF) to EGFR initiates a complex biological response, which includes self-phosphorylation of the receptor due to an intrinsic tyrosine kinase activity, phosphorylation of other membrane proteins, increased intake of metabolites, and increased proliferation. Complete amino acid sequence of EGFR revealed a high degree of homology with viral oncogenes and allowed tentative identification of an external hormone binding domain, a transmembrane domain, and a cytoplasmic domain that includes tyrosine kinase activity. EGF binding induces rapid aggregation of EGFR, a process which was also observed on other receptor systems. These and other observations led to a hypothesis that microaggregation of EGFR is a necessary prerequisite for the biological response of EGF. A direct approach to study the processes of oligomerization of cell membrane proteins is to measure their mobility under various conditions. The lateral mobility of the EGFR was studied on mouse 3T3 fibroblasts and on A431 cells. However, an examination of the equations for the lateral and rotational diffusion in membranes shows that only rotational diffusion is strongly dependent on the size of the diffusing entity. A method of measuring protein rotational diffusion by time-resolved phosphorescence has proved to be very useful in the analysis of both in vivo and in vitro systems. The authors apply this method to study the mobility of EGFR on living A431 cells and membrane preparations.

Paper Details

Date Published: 1 June 1991
PDF: 6 pages
Proc. SPIE 1432, Biomolecular Spectroscopy II, (1 June 1991); doi: 10.1117/12.44211
Show Author Affiliations
Raphael Zidovetzki, Univ. of California/Riverside (United States)
David Allen Johnson, Univ. of California/Riverside (United States)
Donna J. Arndt-Jovin, Max-Planck-Institute for Biophysical Chemistry (Germany)
Thomas M. Jovin, Max-Planck-Institute for Biophysical Chemistry (Germany)


Published in SPIE Proceedings Vol. 1432:
Biomolecular Spectroscopy II
Robert R. Birge; Laurence A. Nafie, Editor(s)

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