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Epidermal growth factor receptor (EGFR) signal transduction is initiated via ligand (EGF) binding, followed by dimerization, autophosphorylation of the C-terminal tails, and recruitment of proteins that form a larger signaling complex to propagate the signal. We explored the relationship between receptor mobility and signaling using single-particle tracking (SPT) by examining the diffusional dynamics of EGFR and two truncation mutants to understand whether mobility changes are correlated with signaling. Results revealed that phosphorylation of the C-terminal tail of EGFR is required for maximal reduction in mobility that occurs with EGF stimulation, indicating that receptor mobility is a read-out for receptor signaling. Additionally, this study looks at the relationship between EGFR and another membrane receptor, Recepteur d’Origine Nantis (RON), using the same approach. By tracking the diffusional dynamics of RON, we found that RON’s kinase domain is not required for EGF-dependent slowdown and that EGFR phosphorylates RON to propagate crosstalk.