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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Antibody-based analysis reveals "filamentous vs. non-filamentous" and "cytoplasmic vs. nuclear" crosstalk of cytoskeletal proteins

Masahiro Kumeta et al. Exp Cell Res. 2013.

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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.

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