The dystrophia myotonica WD repeat‐containing protein DMWD and WDR20 differentially regulate USP12 deubiquitinase

FEBS Journal ◽  
2021 ◽  
Author(s):  
Anne Olazabal‐Herrero ◽  
Martin Bilbao‐Arribas ◽  
Onintza Carlevaris ◽  
Maria Sendino ◽  
Endika Varela‐Martinez ◽  
...  
1964 ◽  
Vol 148 (5) ◽  
pp. 290-303 ◽  
Author(s):  
D.H. Böhme ◽  
H. Hippius
Keyword(s):  

Author(s):  
Anja Dölle ◽  
Bikash Adhikari ◽  
Andreas Krämer ◽  
Janik Weckesser ◽  
Nicola Berner ◽  
...  
Keyword(s):  

2020 ◽  
Vol 48 (12) ◽  
pp. 6583-6596
Author(s):  
Akiko Fujimura ◽  
Yuki Hayashi ◽  
Kazashi Kato ◽  
Yuichiro Kogure ◽  
Mutsuro Kameyama ◽  
...  

Abstract The nucleolus is a membrane-less nuclear structure that disassembles when cells undergo mitosis. During mitosis, nucleolar factors are thus released from the nucleolus and dynamically change their subcellular localization; however, their functions remain largely uncharacterised. Here, we found that a nucleolar factor called nucleolar protein 11 (NOL11) forms a protein complex with two tryptophan-aspartic acid (WD) repeat proteins named WD-repeat protein 43 (WDR43) and Cirhin in mitotic cells. This complex, referred to here as the NWC (NOL11-WDR43-Cirhin) complex, exists in nucleoli during interphase and translocates to the periphery of mitotic chromosomes, i.e., perichromosomal regions. During mitotic progression, both the congression of chromosomes to the metaphase plate and sister chromatid cohesion are impaired in the absence of the NWC complex, as it is required for the centromeric enrichment of Aurora B and the associating phosphorylation of histone H3 at threonine 3. These results reveal the characteristics of a novel protein complex consisting of nucleolar proteins, which is required for regulating kinetochores and centromeres to ensure faithful chromosome segregation.


2004 ◽  
Vol 24 (7) ◽  
pp. 2932-2943 ◽  
Author(s):  
Hailing Cheng ◽  
Xiaoyuan He ◽  
Claire Moore

ABSTRACT Swd2, an essential WD repeat protein in Saccharomyces cerevisiae, is a component of two very different complexes: the cleavage and polyadenylation factor CPF and the Set1 methylase, which modifies lysine 4 of histone H3 (H3-K4). It was not known if Swd2 is important for the function of either of these entities. We show here that, in extract from cells depleted of Swd2, cleavage and polyadenylation of the mRNA precursor in vitro are completely normal. However, temperature-sensitive mutations or depletion of Swd2 causes termination defects in some genes transcribed by RNA polymerase II. Overexpression of Ref2, a protein previously implicated in snoRNA 3′ end formation and Swd2 recruitment to CPF, can rescue the growth and termination defects, indicating a functional interaction between the two proteins. Some swd2 mutations also significantly decrease global H3-K4 methylation and cause other phenotypes associated with loss of this chromatin modification, such as loss of telomere silencing, hydroxyurea sensitivity, and alterations in repression of INO1 transcription. Even though the two Swd2-containing complexes are both localized to actively transcribed genes, the allele specificities of swd2 defects suggest that the functions of Swd2 in mediating RNA polymerase II termination and H3-K4 methylation are not tightly coupled.


Genomics ◽  
2000 ◽  
Vol 63 (3) ◽  
pp. 391-399 ◽  
Author(s):  
Catherine L. Taylor Clelland ◽  
Liviu Craciun ◽  
Carter Bancroft ◽  
Thomas Lufkin

2010 ◽  
Vol 10 (1) ◽  
pp. 134 ◽  
Author(s):  
Damien Chevanne ◽  
Sven J Saupe ◽  
Corinne Clavé ◽  
Mathieu Paoletti

1977 ◽  
Vol 34 (2) ◽  
pp. 199-211 ◽  
Author(s):  
John N. Walton ◽  
Dorothy Irving ◽  
B.E. Tomlinson

2009 ◽  
Vol 13 (10) ◽  
pp. 2673-2684 ◽  
Author(s):  
Zhihong Cheng ◽  
Yuying Liu ◽  
Chernhoe Wang ◽  
Roy Parker ◽  
Haiwei Song

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