Identification of an FMNL2 Interactome by Quantitative Mass Spectrometry

Author:

Fox Sarah1,Gaudreau-LaPierre Antoine1ORCID,Reshke Ryan1,Podinic Irina1,Gibbings Derrick J.1,Trinkle-Mulcahy Laura1,Copeland John W.1

Affiliation:

1. Department of Cellular and Molecular Medicine, Faculty of Medicine, University of Ottawa, Ottawa, ON K1H 8M5, Canada

Abstract

Formin Homology Proteins (Formins) are a highly conserved family of cytoskeletal regulatory proteins that participate in a diverse range of cellular processes. FMNL2 is a member of the Diaphanous-Related Formin sub-group, and previous reports suggest FMNL2’s role in filopodia assembly, force generation at lamellipodia, subcellular trafficking, cell–cell junction assembly, and focal adhesion formation. How FMNL2 is recruited to these sites of action is not well understood. To shed light on how FMNL2 activity is partitioned between subcellular locations, we used biotin proximity labeling and proteomic analysis to identify an FMNL2 interactome. The interactome identified known and new FMNL2 interacting proteins with functions related to previously described FMNL2 activities. In addition, our interactome predicts a novel connection between FMNL2 and extracellular vesicle assembly. We show directly that FMNL2 protein is present in exosomes.

Funder

Canadian Institutes of Health Research

Publisher

MDPI AG

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