Sortilin limits EGFR signaling by promoting its internalization in lung cancer

Hussein Al-Akhrass, Thomas Naves (), François Vincent, Amandine Magnaudeix, Karine Durand, François Bertin, Boris Melloni, Marie-Odile Jauberteau and Fabrice Lalloué
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Hussein Al-Akhrass: Université de Limoges, Faculté de Médecine
Thomas Naves: Université de Limoges, Faculté de Médecine
François Vincent: Université de Limoges, Faculté de Médecine
Amandine Magnaudeix: Université de Limoges, Faculté de Médecine
Karine Durand: Université de Limoges, Faculté de Médecine
François Bertin: Centre Hospitalier et Universitaire de Limoges
Boris Melloni: Centre Hospitalier et Universitaire de Limoges
Marie-Odile Jauberteau: Université de Limoges, Faculté de Médecine
Fabrice Lalloué: Université de Limoges, Faculté de Médecine

Nature Communications, 2017, vol. 8, issue 1, 1-15

Abstract: Abstract Tyrosine kinase receptors such as the epidermal growth factor receptor (EGFR) transduce information from the microenvironment into the cell and activate homeostatic signaling pathways. Internalization and degradation of EGFR after ligand binding limits the intensity of proliferative signaling, thereby helping to maintain cell integrity. In cancer cells, deregulation of EGFR trafficking has a variety of effects on tumor progression. Here we report that sortilin is a key regulator of EGFR internalization. Loss of sortilin in tumor cells promoted cell proliferation by sustaining EGFR signaling at the cell surface, ultimately accelerating tumor growth. In lung cancer patients, sortilin expression decreased with increased pathologic grade, and expression of sortilin was strongly correlated with survival, especially in patients with high EGFR expression. Sortilin is therefore a regulator of EGFR intracellular trafficking that promotes receptor internalization and limits signaling, which in turn impacts tumor growth.

Date: 2017
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DOI: 10.1038/s41467-017-01172-5

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