MAZUR, Antonina Joanna, Tomasz Witold RADASZKIEWICZ, Aleksandra MAKOWIECKA, Maria MALICKA-BLASZKIEWICZ, Hans Georg MANNHERZ a Dorota NOWAK. Gelsolin interacts with LamR, hnRNP U, nestin, Arp3 and beta-tubulin in human melanoma cells as revealed by immunoprecipitation and mass spectrometry. European Journal of Cell Biology. Jena: Elsevier GMBH, 2016, roč. 95, č. 1, s. 26-41. ISSN 0171-9335. Dostupné z: https://dx.doi.org/10.1016/j.ejcb.2015.11.001.
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Základní údaje
Originální název Gelsolin interacts with LamR, hnRNP U, nestin, Arp3 and beta-tubulin in human melanoma cells as revealed by immunoprecipitation and mass spectrometry
Autoři MAZUR, Antonina Joanna, Tomasz Witold RADASZKIEWICZ (616 Polsko, domácí), Aleksandra MAKOWIECKA, Maria MALICKA-BLASZKIEWICZ, Hans Georg MANNHERZ a Dorota NOWAK.
Vydání European Journal of Cell Biology, Jena, Elsevier GMBH, 2016, 0171-9335.
Další údaje
Originální jazyk angličtina
Typ výsledku Článek v odborném periodiku
Obor 10601 Cell biology
Stát vydavatele Německo
Utajení není předmětem státního či obchodního tajemství
WWW Full Text
Impakt faktor Impact factor: 3.712
Kód RIV RIV/00216224:14310/16:00111736
Organizační jednotka Přírodovědecká fakulta
Doi http://dx.doi.org/10.1016/j.ejcb.2015.11.001
UT WoS 000371563200003
Klíčová slova anglicky Gelsolin; actbl2; LamR; hnRNP U; Nestin; beta Tubulin
Štítky rivok
Příznaky Mezinárodní význam, Recenzováno
Změnil Změnila: Mgr. Marie Šípková, DiS., učo 437722. Změněno: 16. 12. 2019 17:37.
Anotace
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.
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