Rotational diffusion of receptors for epidermal growth factor measured by time-resolved phosphorescence depolarization

Raphael Zidovetzki; David Allen Johnson; Donna J. Arndt-Jovin; Thomas M. Jovin

doi:10.1117/12.44211

1 June 1991 Rotational diffusion of receptors for epidermal growth factor measured by time-resolved phosphorescence depolarization

Raphael Zidovetzki, David Allen Johnson, Donna J. Arndt-Jovin, Thomas M. Jovin

Author Affiliations +

Proceedings Volume 1432, Biomolecular Spectroscopy II; (1991) https://doi.org/10.1117/12.44211
Event: Optics, Electro-Optics, and Laser Applications in Science and Engineering, 1991, Los Angeles, CA, United States

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.

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Raphael Zidovetzki, David Allen Johnson, Donna J. Arndt-Jovin, and Thomas M. Jovin "Rotational diffusion of receptors for epidermal growth factor measured by time-resolved phosphorescence depolarization", Proc. SPIE 1432, Biomolecular Spectroscopy II, (1 June 1991); https://doi.org/10.1117/12.44211

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KEYWORDS

Receptors

Phosphorescence

Diffusion

Picosecond phenomena

Proteins

Fluorescence anisotropy

Anisotropy

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