Detailed Information on Publication Record
2016
Gelsolin interacts with LamR, hnRNP U, nestin, Arp3 and beta-tubulin in human melanoma cells as revealed by immunoprecipitation and mass spectrometry
MAZUR, Antonina Joanna, Tomasz Witold RADASZKIEWICZ, Aleksandra MAKOWIECKA, Maria MALICKA-BLASZKIEWICZ, Hans Georg MANNHERZ et. al.Basic information
Original name
Gelsolin interacts with LamR, hnRNP U, nestin, Arp3 and beta-tubulin in human melanoma cells as revealed by immunoprecipitation and mass spectrometry
Authors
MAZUR, Antonina Joanna, Tomasz Witold RADASZKIEWICZ (616 Poland, belonging to the institution), Aleksandra MAKOWIECKA, Maria MALICKA-BLASZKIEWICZ, Hans Georg MANNHERZ and Dorota NOWAK
Edition
European Journal of Cell Biology, Jena, Elsevier GMBH, 2016, 0171-9335
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10601 Cell biology
Country of publisher
Germany
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Impact factor
Impact factor: 3.712
RIV identification code
RIV/00216224:14310/16:00111736
Organization unit
Faculty of Science
UT WoS
000371563200003
Keywords in English
Gelsolin; actbl2; LamR; hnRNP U; Nestin; beta Tubulin
Tags
Tags
International impact, Reviewed
Změněno: 16/12/2019 17:37, Mgr. Marie Šípková, DiS.
Abstract
V originále
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.