Structure and Function of Nopp140 and Treacle

He, Fang

doi:10.1007/978-1-4614-0514-6_11

Cited by 8 publications

(8 citation statements)

References 181 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Nopp-140 and, in a lesser extent, p80/cofilin were also found in the post-nuclear. These proteins are known to shuttle between the nucleus and the cytoplasm [ 62 ; 63 ]. The nuclear fraction was free of the cis -Golgi apparatus marker GM130 and cytosolic protein GAPDH but positive for calnexin and flotillin-1 ( Fig 3A ).…”

Section: Resultsmentioning

confidence: 99%

“…Our confocal microscopy studies demonstrated the co-localization of Cx46 with Nopp-140. Nopp-140 is a phosphoprotein shuttling between the cytoplasm and the nucleus where it associates preferentially with the nucleolus (see review on Nopp-140 [ 63 ]). In the nucleolus, Nopp-140 localizes to the fibrillar center (FC) and dense fibrillar center (DFC) never to the granular compartment (GC).…”

Section: Discussionmentioning

confidence: 99%

“…All these actions support the view of Nopp-140 engagement in nucleolus functioning particularly in rRNA biogenesis. Nopp-140 also localizes to Cajal bodies where it interacts with snoRNPs and with p80/coilin (reviewed in [ 63 ]. Since we did not detect co-localization of Cx46 with p80/coilin, Nopp-140-Cx46 interaction is likely taking place in the nucleolus and suggests involvement of Cx46 or its cooperation in Nopp-140-mediated activities such as the synthesis and modification of rRNA.…”

Section: Discussionmentioning

confidence: 99%

See 2 more Smart Citations

Distinctive actions of connexin 46 and connexin 50 in anterior pituitary folliculostellate cells

et al. 2017

View full text Add to dashboard Cite

Folliculostellate cell gap junctions establish a network for the transmission of information within the anterior pituitary. Connexins make up gap junction channels. Changes in connexin (Cx) turnover modify gap junction-mediated intercellular communication. We have reported that cytokines and hormones influence Cx43 turnover and coupling in folliculostellate cells and in the folliculostellate cell line TtT/GF. In addition, the expression of different connexins alters intercellular communication and connexins may have functions besides cell coupling. Here we assessed the expression, turnover and subcellular localization of Cx46 and Cx50 in the anterior pituitary and TtT/GF cells. Then, we assessed the impact of various natural (lactation, annual reproductive cycle, bFGF) and pathological (autoimmune orchitis, diabetes/obesity) conditions associated with altered anterior pituitary hormone secretion on Cx46 and Cx50. Anterior pituitary Cx46 and Cx50 expression and subcellular distribution were cell-dependent. Cx46 was expressed by folliculostellate, TtT/GF and endocrine cells. In the cytoplasm, Cx46 was chiefly associated with lysosomes. Variously sized Cx46 molecules were recovered exclusively in the TtT/GF cell nuclear fraction. In the nucleus, Cx46 co-localized with Nopp-140, a nucleolar factor involved in rRNA processing. Neither cytoplasmic nor nuclear Cx46 and Cx43 co-localized. Cx50 localized to folliculostellate and TtT/GF cells, and to the walls of blood capillaries, not to endocrine cells. Cx50 was cytoplasmic and associated with the cell membrane, not nuclear. Cx50 did not co-localize with Cx46 but it co-localized in the cytoplasm and co-immunoprecipitated with Cx43. Cx46 and Cx50 responses to various physiological and pathological challenges were different, often opposite. Cx46 and Cx43 expression and phosphorylation profiles differed in the anterior pituitary, whereas Cx50 and Cx43 were similar. The data suggest that Cx46 participates to cellular growth and proliferation and that Cx50, together with Cx43, contributes to folliculostellate cell coupling.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Distinctive actions of connexin 46 and connexin 50 in anterior pituitary folliculostellate cells

et al. 2017

View full text Add to dashboard Cite

show abstract

“…4 Both proteins are over 100 kDa in size, both contain LisH dimerization motifs in their N-terminal region, and both proteins contain a large central domain consisting of alternating acidic and basic motifs with similar amino acid compositions; the acidic motifs are rich in Glu, Asp and phospho-Ser, while the basic motifs are rich in Lys and Pro. Both proteins are believed to function as chaperones for snoRNP complexes as these complexes direct site-specific methylation and pseudouridylation of pre-rRNA within the dense fibrillar regions of eukaryotic nucleoli.…”

Section: Uas-c42/uas-c42; P53δ/p53δ (Rnai) (Lane 4) (B) the Cross mentioning

confidence: 99%

Nucleolar stress in Drosophila melanogaster

James

Cindass²,

Mayer³

et al. 2013

Nucleus

Self Cite

View full text Add to dashboard Cite

“…Subsequent work showed that Nopp140 associates with C/D box small nucleolar ribonucleoprotein (snoRNPs) that guide nucleotide-specific 2′-O-methylation of the pre-rRNA, and with H/ACA box snoRNPs that direct site-specific pseudouridylation of pre-rRNA and snRNAs (Yang et al 2000). These interactions with Nopp140 may initiate within CBs as Nopp140 is thought to shuttle these snoRNPs from CBs to nucleoli (Isaac et al 1998;Yang et al 2000;Wang et al 2002;Meier 2005;Lo et al 2006;He and DiMario 2011). Nopp140 also interacts with RNA Pol I to regulate rRNA transcription, perhaps linking RNA Pol I transcription with pre-rRNA processing (Chen et al 1999;Meier 2005).…”

Section: Introductionmentioning

confidence: 99%

The Nopp140 gene in Drosophila melanogaster displays length polymorphisms in its large repetitive second exon

Baral

2019

Mol Genet Genomics

View full text Add to dashboard Cite

Nopp140, often called the nucleolar and Cajal body phosphoprotein (NOLC1), is an evolutionarily conserved chaperone for the transcription and processing of rRNA during ribosome subunit assembly. Metazoan Nopp140 contains an amino terminal LisH dimerization domain and a highly conserved carboxyl domain. A large central domain consists of alternating basic and acidic motifs of low sequence complexity. Orthologous versions of Nopp140 contain variable numbers of repeating basic-acidic units. While vertebrate Nopp140 genes use multiple exons to encode the central domain, the Nopp140 gene in Drosophila uses exclusively exon 2 to encode the central domain. Here, we define three overlapping repeat sequence patterns (P, P′, and P″) within the central domain of D. melanogaster Nopp140. These repeat patterns are poorly conserved in other Drosophila species. We also describe a length polymorphism in exon 2 that pertains specifically to the P′ pattern in D. melanogaster. The pattern displays either two or three 96 base pair repeats, respectively, referred to as Nopp140-Short and Nopp140-Long. Fly lines homozygous for one or the other allele, or heterozygous for both alleles, show no discernible phenotypes. PCR characterization of the long and short alleles shows a poorly defined, artifactual bias toward amplifying the long allele over the short allele. The significance of this polymorphism will be in discerning the largely unknown properties of Nopp140's large central domain in rDNA transcription and ribosome biogenesis.

show abstract

Structure and Function of Nopp140 and Treacle

Cited by 8 publications

References 181 publications

Distinctive actions of connexin 46 and connexin 50 in anterior pituitary folliculostellate cells

Distinctive actions of connexin 46 and connexin 50 in anterior pituitary folliculostellate cells

Nucleolar stress in Drosophila melanogaster

The Nopp140 gene in Drosophila melanogaster displays length polymorphisms in its large repetitive second exon

Contact Info

Product

Resources

About