Antibody-based analysis reveals "filamentous vs. non-filamentous" and "cytoplasmic vs. nuclear" crosstalk of cytoskeletal proteins - PubMed (original) (raw)
. 2013 Dec 10;319(20):3226-37.
doi: 10.1016/j.yexcr.2013.07.021. Epub 2013 Aug 1.
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- PMID: 23911988
- DOI: 10.1016/j.yexcr.2013.07.021
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Antibody-based analysis reveals "filamentous vs. non-filamentous" and "cytoplasmic vs. nuclear" crosstalk of cytoskeletal proteins
Masahiro Kumeta et al. Exp Cell Res. 2013.
Free article
Abstract
To uncover the molecular composition and dynamics of the functional scaffold for the nucleus, three fractions of biochemically-stable nuclear protein complexes were extracted and used as immunogens to produce a variety of monoclonal antibodies. Many helix-based cytoskeletal proteins were identified as antigens, suggesting their dynamic contribution to nuclear architecture and function. Interestingly, sets of antibodies distinguished distinct subcellular localization of a single isoform of certain cytoskeletal proteins; distinct molecular forms of keratin and actinin were found in the nucleus. Their nuclear shuttling properties were verified by the apparent nuclear accumulations under inhibition of CRM1-dependent nuclear export. Nuclear keratins do not take an obvious filamentous structure, as was revealed by non-filamentous cytoplasmic keratin-specific monoclonal antibody. These results suggest the distinct roles of the helix-based cytoskeletal proteins in the nucleus.
Keywords: Cytoskeleton; EGFP; Keratin; LMB; Monoclonal antibody; NES; NLS; NPC; Nuclear matrix; Nuclear scaffold; Nuclear transport; enhanced-GFP; leptomycin B; nuclear export signal; nuclear localization signal; nuclear pore complex.
Copyright © 2013 Elsevier Inc. All rights reserved.
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