The actin family protein ARP6 contributes to the structure and the function of the nucleolus.
The actin family protein ARP6 contributes to the structure and the function of the nucleolus.
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DOI:
10.1016/j.bbrc.2015.07.005
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发表时间:
2015-08-21
影响因子:
3.1
通讯作者:
Harata M
中科院分区:
文献类型:
--
作者:
Kitamura H;Matsumori H;Kalendova A;Hozak P;Goldberg IG;Nakao M;Saitoh N;Harata M
The actin family members, consisting of actin and actin-related proteins (ARPs), are essential components of chromatin remodeling complexes. ARP6, one of the nuclear ARPs, is part of the Snf-2-related CREB-binding protein activator protein (SRCAP) chromatin remodeling complex, which promotes the deposition of the histone variant H2A.Z into the chromatin. In this study, we showed that ARP6 influences the structure and the function of the nucleolus. ARP6 is localized in the central region of the nucleolus, and its knockdown induced a morphological change in the nucleolus. We also found that in the presence of high concentrations of glucose ARP6 contributed to the maintenance of active ribosomal DNA (rDNA) transcription by placing H2A.Z into the chromatin. In contrast, under starvation, ARP6 was required for cell survival through the repression of rDNA transcription independently of H2A.Z. These findings reveal novel pleiotropic roles for the actin family in nuclear organization and metabolic homeostasis.
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影响因子:
14.9
作者:
Matsuda R;Hori T;Kitamura H;Takeuchi K;Fukagawa T;Harata M
通讯作者:
Harata M
影响因子:
15.9
作者:
Hetman M;Pietrzak M
通讯作者:
Pietrzak M
DOI:
10.1073/pnas.0909873106
发表时间:
2009-10-20
影响因子:
11.1
作者:
Hoppe, Sven;Bierhoff, Holger;Voit, Renate
通讯作者:
Voit, Renate
影响因子:
48
作者:
Eliceiri, Kevin W.;Berthold, Michael R.;Goldberg, Ilya G.;Ibanez, Luis;Manjunath, B. S.;Martone, Maryann E.;Murphy, Robert F.;Peng, Hanchuan;Plant, Anne L.;Roysam, Badrinath;Stuurmann, Nico;Swedlow, Jason R.;Tomancak, Pavel;Carpenter, Anne E.
通讯作者:
Carpenter, Anne E.
影响因子:
3.7
作者:
Johnston, Josiah;Iser, Wendy B.;Chow, David K.;Goldberg, Ilya G.;Wolkow, Catherine A.
通讯作者:
Wolkow, Catherine A.