Ultrastructural localization of actin and actin-binding proteins in the nucleus
Jazyk angličtina Země Německo Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
- MeSH
- aktinin MeSH
- aktiny analýza MeSH
- buněčné jádro chemie ultrastruktura MeSH
- HeLa buňky MeSH
- jaderné proteiny analýza MeSH
- lidé MeSH
- lymfocyty chemie ultrastruktura MeSH
- mikrofilamentové proteiny analýza MeSH
- paxilin MeSH
- proteiny aktivující GTPasu MeSH
- spektrin MeSH
- tropomyosin MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- aktinin MeSH
- aktiny MeSH
- jaderné proteiny MeSH
- mikrofilamentové proteiny MeSH
- paxilin MeSH
- proteiny aktivující GTPasu MeSH
- rho GTPase-activating protein MeSH Prohlížeč
- spektrin MeSH
- tropomyosin MeSH
Nuclear actin plays an important role in such processes as chromatin remodeling, transcriptional regulation, RNA processing, and nuclear export. Recent research has demonstrated that actin in the nucleus probably exists in dynamic equilibrium between monomeric and polymeric forms, and some of the actin-binding proteins, known to regulate actin dynamics in cytoplasm, have been also shown to be present in the nucleus. In this paper, we present ultrastructural data on distribution of actin and various actin-binding proteins (alpha-actinin, filamin, p190RhoGAP, paxillin, spectrin, and tropomyosin) in nuclei of HeLa cells and resting human lymphocytes. Probing extracts of HeLa cells for the presence of actin-binding proteins also confirmed their presence in nuclei. We report for the first time the presence of tropomyosin and p190RhoGAP in the cell nucleus, and the spatial colocalization of actin with spectrin, paxillin, and alpha-actinin in the nucleolus.
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