Intersectin adaptor proteins are associated with actin-regulating protein WIP in invadopodia

Cellular Signalling
Tetyana GryaznovaAlla Rynditch

Abstract

Invasive cancer cells form actin-rich membrane protrusions called invadopodia that degrade extracellular matrix and facilitate cell invasion and metastasis. WIP (WASP-interacting protein) together with N-WASP (neural Wiskott-Aldrich syndrome protein) are localized in invadopodia and play a crucial role in their formation. Here we show that WIP interacts with endocytic adaptor proteins of the intersectin (ITSN) family, ITSN1 and ITSN2. The interaction is mediated by the SH3 domains of ITSNs and the middle part of the WIP proline-rich motifs. We have also demonstrated that ITSN1, WIP and N-WASP can form a complex in cells. Endogenous ITSN1 and ITSN2 are located in invasive protrusions of MDA-MB-231 breast cancer cell line. Moreover, data from immunofluorescent analysis revealed co-localization of ITSN1 and WIP at sites of invadopodia formation and in clathrin-coated pits. Together, these findings provide insights into the molecular mechanisms of invadopodia formation and identify ITSNs as scaffold proteins involved in this process.

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Citations

Oct 18, 2016·Biochimica Et Biophysica Acta. Molecular Cell Research·Erika Herrero-Garcia, John P O'Bryan
Jun 11, 2017·The Journal of Biological Chemistry·Magda Nohemí Hernández-VásquezJosé Vázquez-Prado
Mar 31, 2018·The Biochemical Journal·Gualtiero AlvisiAnnalisa Radeghieri
Jun 20, 2017·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Jiaqi ZhangQiang Wang
May 14, 2020·Proceedings of the National Academy of Sciences of the United States of America·Ruth X WangSean P Colgan

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