Nuclear structures surrounding internal lamin invaginations
© 2013 Wiley Periodicals, Inc..
A- and C-type lamins are intermediate filament proteins responsible for the maintenance of nuclear shape and most likely nuclear architecture. Here, we propose that pronounced invaginations of A/C-type lamins into the nuclear interior represent channels for the transport of regulatory molecules to and from nuclear and nucleolar regions. Using fluorescent protein technology and immunofluorescence, we show that A-type lamin channels interact with several nuclear components, including fibrillarin- and UBF-positive regions of nucleoli, foci of heterochromatin protein 1 β, polycomb group bodies, and genomic regions associated with DNA repair. Similar associations were observed between A/C-type lamin channels and nuclear pores, lamin-associated protein LAP2α, and promyelocytic leukemia nuclear bodies. Interestingly, regions with high levels of A/C-type lamins had low levels of B-type lamins, and vice versa. These characteristics were observed in primary and immortalized mouse embryonic fibroblasts as well as human and mouse embryonic stem cell colonies exhibiting stem cell-specific lamin positivity. Our findings indicate that internal channels formed by nuclear lamins likely contribute to normal cellular processes through association with various nuclear and nucleolar structures.
Medienart: |
E-Artikel |
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Erscheinungsjahr: |
2014 |
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Erschienen: |
2014 |
Enthalten in: |
Zur Gesamtaufnahme - volume:115 |
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Enthalten in: |
Journal of cellular biochemistry - 115(2014), 3 vom: 23. März, Seite 476-87 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Legartová, Soňa [VerfasserIn] |
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Links: |
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Anmerkungen: |
Date Completed 20.10.2014 Date Revised 04.03.2014 published: Print Citation Status MEDLINE |
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doi: |
10.1002/jcb.24681 |
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funding: |
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Förderinstitution / Projekttitel: |
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PPN (Katalog-ID): |
NLM231677111 |
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520 | |a A- and C-type lamins are intermediate filament proteins responsible for the maintenance of nuclear shape and most likely nuclear architecture. Here, we propose that pronounced invaginations of A/C-type lamins into the nuclear interior represent channels for the transport of regulatory molecules to and from nuclear and nucleolar regions. Using fluorescent protein technology and immunofluorescence, we show that A-type lamin channels interact with several nuclear components, including fibrillarin- and UBF-positive regions of nucleoli, foci of heterochromatin protein 1 β, polycomb group bodies, and genomic regions associated with DNA repair. Similar associations were observed between A/C-type lamin channels and nuclear pores, lamin-associated protein LAP2α, and promyelocytic leukemia nuclear bodies. Interestingly, regions with high levels of A/C-type lamins had low levels of B-type lamins, and vice versa. These characteristics were observed in primary and immortalized mouse embryonic fibroblasts as well as human and mouse embryonic stem cell colonies exhibiting stem cell-specific lamin positivity. Our findings indicate that internal channels formed by nuclear lamins likely contribute to normal cellular processes through association with various nuclear and nucleolar structures | ||
650 | 4 | |a Journal Article | |
650 | 4 | |a Research Support, Non-U.S. Gov't | |
650 | 4 | |a CHROMATIN | |
650 | 4 | |a DNA REPAIR | |
650 | 4 | |a ES CELLS | |
650 | 4 | |a HP1 PROTEIN | |
650 | 4 | |a LAMINS | |
650 | 4 | |a NUCLEAR PORES | |
650 | 4 | |a PML BODIES | |
650 | 4 | |a TRANSCRIPTION | |
650 | 7 | |a Chromosomal Proteins, Non-Histone |2 NLM | |
650 | 7 | |a DNA-Binding Proteins |2 NLM | |
650 | 7 | |a Lamin Type A |2 NLM | |
650 | 7 | |a Lamin Type B |2 NLM | |
650 | 7 | |a Membrane Proteins |2 NLM | |
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700 | 1 | |a Kozubek, Stanislav |e verfasserin |4 aut | |
700 | 1 | |a Sehnalová, Petra |e verfasserin |4 aut | |
700 | 1 | |a Bártová, Eva |e verfasserin |4 aut | |
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