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dc.creatorMorales-Urteaga, X. (Xabier)-
dc.creatorPeláez, R. (Rafael)-
dc.creatorGarasa, S. (Saray)-
dc.creatorOrtiz-de-Solorzano, C. (Carlos)-
dc.creatorRouzaut, A. (Ana)-
dc.date.accessioned2022-01-25T14:59:28Z-
dc.date.available2022-01-25T14:59:28Z-
dc.date.issued2021-
dc.identifier.citationMorales-Urteaga, X. (Xabier); Peláez, R.; Garasa, S.; et al. "CRMP2 as a candidate target to interfere with lung cancer cell migration". Biomolecules. 11 (10), 2021, 1533es
dc.identifier.issn2218-273X-
dc.identifier.urihttps://hdl.handle.net/10171/62845-
dc.description.abstractCollapsin response mediator protein 2 (CRMP2) is an adaptor protein that adds tubulin dimers to the growing tip of a microtubule. First described in neurons, it is now considered a ubiquitous protein that intervenes in processes such as cytoskeletal remodeling, synaptic connection and trafficking of voltage channels. Mounting evidence supports that CRMP2 plays an essential role in neuropathology and, more recently, in cancer. We have previously described a positive correlation between nuclear phosphorylation of CRMP2 and poor prognosis in lung adenocarcinoma patients. In this work, we studied whether this cytoskeleton molding protein is involved in cancer cell migration. To this aim, we evaluated CRMP2 phosphorylation and localization in the extending lamella of lung adenocarcinoma migrating cells using in vitro assays and in vivo confocal microscopy. We demonstrated that constitutive phosphorylation of CRMP2 impaired lamella formation, cell adhesion and oriented migration. In search of a mechanistic explanation of this phenomenon, we discovered that CRMP2 Ser522 phospho-mimetic mutants display unstable tubulin polymers, unable to bind EB1 plus-Tip protein and the cortical actin adaptor IQGAP1. In addition, integrin recycling is defective and invasive structures are less evident in these mutants. Significantly, mouse xenograft tumors of NSCLC expressing CRMP2 phosphorylation mimetic mutants grew significantly less than wild-type tumors.-
dc.description.sponsorshipThis work was funded by MIMECO grant DPI2012-38090-C03-02. X.M. was supported with a phD fellowship of the Basque Country government. Rafael Peláez was supported by MIMECO/Torres Quevedo program PTQ-11-04778. C.O.d.S. was funded by the Spanish Ministry of Science, Innovation and Universities, under grant RTI2018-094494-B-C22 (MCIU/AEI/FEDER, UE)-
dc.language.isoen-
dc.rightsinfo:eu-repo/semantics/openAccess-
dc.subjectCRMP2-
dc.subjectLung cancer-
dc.subjectMigration-
dc.subjectCytoskeleton-
dc.titleCRMP2 as a candidate target to interfere with lung cancer cell migration-
dc.typeinfo:eu-repo/semantics/article-
dc.description.noteThis article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https:// creativecommons.org/licenses/by/ 4.0/).-
dc.identifier.doi10.3390/biom11101533-
dadun.citation.number10-
dadun.citation.publicationNameBiomolecules-
dadun.citation.startingPage1533-
dadun.citation.volume11-

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