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Interactions between the juxtamembrane domain of the EGFR and calmodulin measured by surface plasmon resonance
Linköping University, Faculty of Health Sciences. Linköping University, Department of Medicine and Care, Pharmacology.
Linköping University, Department of Physics, Chemistry and Biology, Sensor Science and Molecular Physics . Linköping University, The Institute of Technology.
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2002 (English)In: Cellular Signalling, ISSN 0898-6568, E-ISSN 1873-3913, Vol. 14, no 12, 1005-1013 p.Article in journal (Refereed) Published
Abstract [en]

One early response to epidermal growth factor receptor (EGFR) activation is an increase in intracellular calcium. We have used surface plasmon resonance (SPR) to study real-time interactions between the intracellular juxtamembrane (JM) region of EGFR and calmodulin. The EGFR-JM (Met644-Phe688) was expressed as a GST fusion protein and immobilised on a sensor chip surface. Calmodulin specifically interacts with EGFR-JM in a calcium-dependent manner with a high on and high off rate. Chemical modification of EGFR-JM by using arginine-selective phenylglyoxal or deletion of the basic segment Arg645-Arg657 inhibits the interaction. Phosphorylation of EGFR-JM by protein kinase C (PKC) or glutamate substitution of Thr654 inhibits the interaction, suggesting that PKC phosphorylation electrostatically interferes with calmodulin binding to basic arginine residues. Calmodulin binding was also inhibited by suramin. Our results suggest that EGFR-JM is essential for epidermal growth factor (EGF)-mediated calcium-calmodulin signalling and for signal integration between other signalling pathways.

Place, publisher, year, edition, pages
2002. Vol. 14, no 12, 1005-1013 p.
National Category
Medical and Health Sciences
URN: urn:nbn:se:liu:diva-27056DOI: 10.1016/S0898-6568(02)00034-7Local ID: 11702OAI: diva2:247607
Available from: 2009-10-08 Created: 2009-10-08 Last updated: 2010-09-06

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Nilsson, Ulrica KLiedberg, BoSvensson, Samuel
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Faculty of Health SciencesPharmacologySensor Science and Molecular Physics The Institute of Technology
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Cellular Signalling
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