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Publication details
Gelsolin interacts with LamR, hnRNP U, nestin, Arp3 and beta-tubulin in human melanoma cells as revealed by immunoprecipitation and mass spectrometry
Authors | |
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Year of publication | 2016 |
Type | Article in Periodical |
Magazine / Source | European Journal of Cell Biology |
MU Faculty or unit | |
Citation | |
Web | Full Text |
Doi | http://dx.doi.org/10.1016/j.ejcb.2015.11.001 |
Keywords | Gelsolin; actbl2; LamR; hnRNP U; Nestin; beta Tubulin |
Description | Gelsolin, a multifunctional actin binding protein, plays a not yet fully understood role in tumorigenesis. Therefore the goal of this study was to identify additional molecular partners of gelsolin in human melanoma cells, separately in the cytoplasmic compartment and cell nuclei. For this purpose we performed immunoprecipitation experiments based on a modified protocol followed by mass spectrometry. The obtained results were confirmed by Western blot analysis, proximity ligation assays and confocal microscopy. As expected gelsolin interacted with actin, in particular we demonstrate its interaction with cytoplasmic beta and gamma actins, and a newly discovered actin isoform, actbl2. As new gelsolin-interacting partners we identified the ribosomal protein Rpsa, also known as a non-integrin laminin receptor (LamR), and the heterogeneous nuclear ribonucleoprotein hnRNP U. Our data furthermore indicate that gelsolin interacts with particular components of the three cytoskeleton systems: nestin (intermediate filaments), Arp3 (actin cytoskeleton) and beta-tubulin (microtubules). We also report for the first time that gelsolin is a constituent of midbodies, a tubulin containing structure formed at the end of cytokinesis. |