PPFIA1 drives active α5β1 integrin recycling and controls fibronectin fibrillogenesis and vascular morphogenesis

Giulia Mana, Fabiana Clapero, Emiliano Panieri, Valentina Panero, Ralph T. Böttcher, Hui-Yuan Tseng, Federico Saltarin, Elena Astanina, Katarzyna I. Wolanska, Mark R. Morgan, Martin J. Humphries, Massimo M. Santoro, Guido Serini () and Donatella Valdembri ()
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Giulia Mana: University of Torino School of Medicine
Fabiana Clapero: University of Torino School of Medicine
Emiliano Panieri: Molecular Biotechnology Center, University of Torino
Valentina Panero: Molecular Biotechnology Center, University of Torino
Ralph T. Böttcher: Max Planck Institute of Biochemistry
Hui-Yuan Tseng: Max Planck Institute of Biochemistry
Federico Saltarin: University of Torino School of Medicine
Elena Astanina: University of Torino School of Medicine
Katarzyna I. Wolanska: Institute of Translational Medicine, University of Liverpool
Mark R. Morgan: Institute of Translational Medicine, University of Liverpool
Martin J. Humphries: Wellcome Trust Centre for Cell-Matrix Research, Faculty of Biology, Medicine & Health, University of Manchester
Massimo M. Santoro: Molecular Biotechnology Center, University of Torino
Guido Serini: University of Torino School of Medicine
Donatella Valdembri: University of Torino School of Medicine

Nature Communications, 2016, vol. 7, issue 1, 1-20

Abstract: Abstract Basolateral polymerization of cellular fibronectin (FN) into a meshwork drives endothelial cell (EC) polarity and vascular remodelling. However, mechanisms coordinating α5β1 integrin-mediated extracellular FN endocytosis and exocytosis of newly synthesized FN remain elusive. Here we show that, on Rab21-elicited internalization, FN-bound/active α5β1 is recycled to the EC surface. We identify a pathway, comprising the regulators of post-Golgi carrier formation PI4KB and AP-1A, the small GTPase Rab11B, the surface tyrosine phosphatase receptor PTPRF and its adaptor PPFIA1, which we propose acts as a funnel combining FN secretion and recycling of active α5β1 integrin from the trans-Golgi network (TGN) to the EC surface, thus allowing FN fibrillogenesis. In this framework, PPFIA1 interacts with active α5β1 integrin and localizes close to EC adhesions where post-Golgi carriers are targeted. We show that PPFIA1 is required for FN polymerization-dependent vascular morphogenesis, both in vitro and in the developing zebrafish embryo.

Date: 2016
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DOI: 10.1038/ncomms13546

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