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Statements

Subject Item
n2:RIV%2F68378050%3A_____%2F14%3A00434269%21RIV15-GA0-68378050
rdf:type
skos:Concept n14:Vysledek
dcterms:description
Although actin monomers polymerize into filaments in the cytoplasm, the form of actin in the nucleus remains elusive. We searched for the form and function of β-actin fused to nuclear localization signal and to enhanced yellow fluorescent protein (EN-actin). Our results reveal that EN-actin is either dispersed in the nucleoplasm (homogenous EN-actin) or forms bundled filaments in the nucleus (EN-actin filaments). Formation of such filaments was not connected with increased EN-actin levels. Among numerous actin-binding proteins tested, only cofilin is recruited to the EN-actin filaments. Overexpression of EN-actin causes increase in the nuclear levels of actin-related protein 3 (Arp3). Although Arp3, a member of actin nucleation complex Arp2/3, is responsible for EN-actin filament nucleation and bundling, the way cofilin affects nuclear EN-actin filaments dynamics is not clear. While cells with homogenous EN-actin maintained unaffected mitosis during which EN-actin re-localizes to the plasma membrane, generation of nuclear EN-actin filaments severely decreases cell proliferation and interferes with mitotic progress. The introduction of EN-actin manifests in two mitotic-inborn defects—formation of binucleic cells and generation of micronuclei—suggesting that cells suffer aberrant cytokinesis and/or impaired chromosomal segregation. In interphase, nuclear EN-actin filaments passed through chromatin region, but do not co-localize with either chromatin remodeling complexes or RNA polymerases I and II. Surprisingly presence of EN-actin filaments was connected with increase in the overall transcription levels in the S-phase by yet unknown mechanism. Taken together, EN-actin can form filaments in the nucleus which affect important cellular processes such as transcription and mitosis. Although actin monomers polymerize into filaments in the cytoplasm, the form of actin in the nucleus remains elusive. We searched for the form and function of β-actin fused to nuclear localization signal and to enhanced yellow fluorescent protein (EN-actin). Our results reveal that EN-actin is either dispersed in the nucleoplasm (homogenous EN-actin) or forms bundled filaments in the nucleus (EN-actin filaments). Formation of such filaments was not connected with increased EN-actin levels. Among numerous actin-binding proteins tested, only cofilin is recruited to the EN-actin filaments. Overexpression of EN-actin causes increase in the nuclear levels of actin-related protein 3 (Arp3). Although Arp3, a member of actin nucleation complex Arp2/3, is responsible for EN-actin filament nucleation and bundling, the way cofilin affects nuclear EN-actin filaments dynamics is not clear. While cells with homogenous EN-actin maintained unaffected mitosis during which EN-actin re-localizes to the plasma membrane, generation of nuclear EN-actin filaments severely decreases cell proliferation and interferes with mitotic progress. The introduction of EN-actin manifests in two mitotic-inborn defects—formation of binucleic cells and generation of micronuclei—suggesting that cells suffer aberrant cytokinesis and/or impaired chromosomal segregation. In interphase, nuclear EN-actin filaments passed through chromatin region, but do not co-localize with either chromatin remodeling complexes or RNA polymerases I and II. Surprisingly presence of EN-actin filaments was connected with increase in the overall transcription levels in the S-phase by yet unknown mechanism. Taken together, EN-actin can form filaments in the nucleus which affect important cellular processes such as transcription and mitosis.
dcterms:title
Nuclear actin filaments recruit cofilin and actin-related protein 3, and their formation is connected with a mitotic block Nuclear actin filaments recruit cofilin and actin-related protein 3, and their formation is connected with a mitotic block
skos:prefLabel
Nuclear actin filaments recruit cofilin and actin-related protein 3, and their formation is connected with a mitotic block Nuclear actin filaments recruit cofilin and actin-related protein 3, and their formation is connected with a mitotic block
skos:notation
RIV/68378050:_____/14:00434269!RIV15-GA0-68378050
n3:aktivita
n15:P n15:I
n3:aktivity
I, P(ED1.1.00/02.0109), P(GAP305/11/2232), P(LD12063)
n3:cisloPeriodika
2
n3:dodaniDat
n8:2015
n3:domaciTvurceVysledku
n5:9793089 n5:9671706 n5:7003374 n5:6705952
n3:druhVysledku
n12:J
n3:duvernostUdaju
n9:S
n3:entitaPredkladatele
n16:predkladatel
n3:idSjednocenehoVysledku
33221
n3:idVysledku
RIV/68378050:_____/14:00434269
n3:jazykVysledku
n18:eng
n3:klicovaSlova
nuclear actin; transcription; mitosis; actin-related protein 3; cofilin
n3:klicoveSlovo
n6:nuclear%20actin n6:mitosis n6:cofilin n6:transcription n6:actin-related%20protein%203
n3:kodStatuVydavatele
DE - Spolková republika Německo
n3:kontrolniKodProRIV
[6FBEC0DA4EB6]
n3:nazevZdroje
Histochemistry and Cell Biology
n3:obor
n13:EB
n3:pocetDomacichTvurcuVysledku
4
n3:pocetTvurcuVysledku
6
n3:projekt
n4:LD12063 n4:ED1.1.00%2F02.0109 n4:GAP305%2F11%2F2232
n3:rokUplatneniVysledku
n8:2014
n3:svazekPeriodika
142
n3:tvurceVysledku
Uličná, Lívia Hozák, Pavel Kalasová, Ilona Yamazaki, S. Harata, M. Kalendová, Alžběta
n3:wos
000339963300003
s:issn
0948-6143
s:numberOfPages
14
n17:doi
10.1007/s00418-014-1243-9