scholarly journals A LIM Domain Protein from Tobacco Involved in Actin-Bundling and Histone Gene Transcription

2013 ◽  
Vol 6 (2) ◽  
pp. 483-502 ◽  
Author(s):  
Danièle Moes ◽  
Sabrina Gatti ◽  
Céline Hoffmann ◽  
Monika Dieterle ◽  
Flora Moreau ◽  
...  
2009 ◽  
Vol 40 (01) ◽  
Author(s):  
J Schessl ◽  
Y Zou ◽  
MJ McGrath ◽  
BS Cowling ◽  
B Maiti ◽  
...  

Metabolism ◽  
2021 ◽  
pp. 154815
Author(s):  
Maria P. Clemente-Olivo ◽  
Jayron J. Habibe ◽  
Mariska Vos ◽  
Roelof Ottenhoff ◽  
Aldo Jongejan ◽  
...  

1989 ◽  
Vol 264 (25) ◽  
pp. 15034-15042 ◽  
Author(s):  
A J van Wijnen ◽  
K L Wright ◽  
J B Lian ◽  
J L Stein ◽  
G S Stein

1993 ◽  
Vol 217 (2) ◽  
pp. 683-690 ◽  
Author(s):  
Peter ZAHRADKA ◽  
Tracy ELLIOT ◽  
Kenneth HOVLAND ◽  
Dawn E. LARSON ◽  
Laura SAWARD

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Tannaz Norizadeh Abbariki ◽  
Zita Gonda ◽  
Denise Kemler ◽  
Pavel Urbanek ◽  
Tabea Wagner ◽  
...  

AbstractThe process of myogenesis which operates during skeletal muscle regeneration involves the activation of muscle stem cells, the so-called satellite cells. These then give rise to proliferating progenitors, the myoblasts which subsequently exit the cell cycle and differentiate into committed precursors, the myocytes. Ultimately, the fusion of myocytes leads to myofiber formation. Here we reveal a role for the transcriptional co-regulator nTRIP6, the nuclear isoform of the LIM-domain protein TRIP6, in the temporal control of myogenesis. In an in vitro model of myogenesis, the expression of nTRIP6 is transiently up-regulated at the transition between proliferation and differentiation, whereas that of the cytosolic isoform TRIP6 is not altered. Selectively blocking nTRIP6 function results in accelerated early differentiation followed by deregulated late differentiation and fusion. Thus, the transient increase in nTRIP6 expression appears to prevent premature differentiation. Accordingly, knocking out the Trip6 gene in satellite cells leads to deregulated skeletal muscle regeneration dynamics in the mouse. Thus, dynamic changes in nTRIP6 expression contributes to the temporal control of myogenesis.


Gene ◽  
1998 ◽  
Vol 216 (1) ◽  
pp. 163-170 ◽  
Author(s):  
Simon Ming Yuen Lee ◽  
Stephen Kwok Wing Tsui ◽  
Kwok Keung Chan ◽  
Merce Garcia-Barcelo ◽  
Mary Miu Yee Waye ◽  
...  

2021 ◽  
pp. mbc.E20-10-0645
Author(s):  
James P. Kemp ◽  
Xiao-Cui Yang ◽  
Zbigniew Dominski ◽  
William F. Marzluff ◽  
Robert J. Duronio

The Histone Locus Body (HLB) is an evolutionarily conserved nuclear body that regulates the transcription and processing of replication-dependent (RD) histone mRNAs, which are the only eukaryotic mRNAs lacking a poly-A tail. Many nuclear bodies contain distinct domains, but how internal organization is related to nuclear body function is not fully understood. Here, we demonstrate using structured illumination microscopy that Drosophila HLBs have a “core-shell” organization in which the internal core contains transcriptionally active RD histone genes. The N-terminus of Mxc, which contains a domain required for Mxc oligomerization, HLB assembly, and RD histone gene expression, is enriched in the HLB core. In contrast, the C-terminus of Mxc is enriched in the HLB outer shell as is FLASH, a component of the active U7 snRNP that co-transcriptionally cleaves RD histone pre-mRNA. Consistent with these results, we show biochemically that FLASH binds directly to the Mxc C-terminal region. In the rapid S-M nuclear cycles of syncytial blastoderm Drosophila embryos, the HLB disassembles at mitosis and reassembles the core-shell arrangement as histone gene transcription is activated immediately after mitosis. Thus, the core-shell organization is coupled to zygotic histone gene transcription, revealing a link between HLB internal organization and RD histone gene expression.


2009 ◽  
Vol 284 (19) ◽  
pp. 13202-13212 ◽  
Author(s):  
Nicole A. Neuman ◽  
Susan Ma ◽  
Gavin R. Schnitzler ◽  
Yan Zhu ◽  
Giorgio Lagna ◽  
...  

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