A. W. Smith

HER4 is a high affinity dimerization partner for all EGFR/HER/ErbB-family proteins

This study uses PIE-FCCS to show HER4 directly interacts with all HER family members in live cells, even without ligands, suggesting HER4 is a preferred dimerization partner.

Phosphatidylinositol (4,5)-bisphosphate drives the formation of EGFR and EphA2 complexes

This study uses PIE-FCCS to show that PIP2 enhances EGFR and EphA2 multimerization in live cells, revealing a role for anionic lipids in RTK interactions.

The SAM Domain of EphA2 Inhibits Ligand-Independent Clustering and Activation

This study investigates the role of the SAM domain in EphA2, showing it inhibits ligand-independent clustering and kinase activity in both full-length and intracellular domain constructs.

Allosteric inhibition of the epidermal growth factor receptor through disruption of transmembrane interactions

This study develops a pH-responsive peptide, PET1, that inhibits EGFR-mediated cell migration by disrupting transmembrane interactions, offering a new strategy for targeting RTKs with reduced side effects.

Allele-specific activation, enzyme kinetics, and inhibitor sensitivities of EGFR exon 19 deletion mutations in lung cancer

The paper identifies allele-specific functional differences among EGFR exon 19 deletion variants, showing how sequence and structure motifs affect oncogenic activity, dimerization, and TKI sensitivity.

Cell Surface Multimeric Assemblies Regulate Canonical and Noncanonical EphA2 Receptor Tyrosine Kinase Signaling

This study identifies molecular interfaces that mediate EphA2 receptor assembly and distinguishes between canonical and noncanonical signaling pathways.

Resolving the Interactions Between Class 3 Semaphorin Receptors in Live Cells

This study uses PIE-FCCS to analyze receptor interactions in live cells, finding that Plexin D1 is monomeric while others form dimers or heteromers, with ligand-induced complex formation only observed for Plexin D1 and neuropilin-1.

Two forms of Opa1 cooperate to complete fusion of the mitochondrial inner-membrane

The paper shows that two forms of Opa1 work together to regulate mitochondrial inner-membrane fusion, with l-Opa1 enabling docking and s-Opa1 facilitating efficient pore opening.