The distribution of phosphorylated SR proteins and alternative splicing are regulated by RANBP2

Saitoh, Noriko; Sakamoto, Chiyomi; Hagiwara, Masatoshi; Agredano-Moreno, Lourdes Teresa; Jiménez‐García, Luis Felipe; Nakao, Mitsuyoshi

doi:10.1091/mbc.e11-09-0783

Cited by 41 publications

(47 citation statements)

References 74 publications

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“…S9). These results are consistent with the localization of SR proteins in both plants and animals to sub-nuclear speckles via the RS domain (Mori et al, 2012;Saitoh et al, 2012;Tillemans et al, 2005;Tillemans et al, 2006;Cazalla et al, 2002).…”

Section: Rbm48 Interacts With U12 and U2 Splicing Factorssupporting

confidence: 88%

RNA Binding Motif Protein 48 is required for U12 splicing and maize endosperm differentiation

Bai

Corll

Shodja

et al. 2018

Preprint

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The last eukaryotic common ancestor had two classes of introns that are still found in most eukaryotic lineages. Common U2-type and rare U12-type introns are spliced by the major and minor spliceosomes, respectively. Relatively few splicing factors have been shown to be specific to the minor spliceosome. We found that the maize RNA Binding Motif Protein48 (RBM48) is a U12 splicing factor that functions to promote cell differentiation and repress cell proliferation. RBM48 is coselected with the U12 splicing factor, ZRSR2/RGH3. Protein-protein interactions between RBM48, RGH3, and U2 Auxiliary Factor (U2AF) subunits suggest major and minor spliceosome factors may form complexes during intron recognition. Human RBM48 interacts with ARMC7.Maize RBM48 and ARMC7 have a conserved protein-protein interaction. These data predict that RBM48 is likely to function in U12 splicing throughout eukaryotes and that U12 splicing promotes endosperm cell differentiation in maize.

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Section: Rbm48 Interacts With U12 and U2 Splicing Factorssupporting

confidence: 88%

RNA Binding Motif Protein 48 is required for U12 splicing and maize endosperm differentiation

Bai

Corll

Shodja

et al. 2018

Preprint

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“…Downregulation of splicing factor SRSF3 induces an alternatively spliced isoform of p53 that promotes cellular senescence [298]. Senescence-associated stress signals result in the cytoplasmic accumulation of several splicing factors such as SRSF1 in endothelial cells [299], their shuttling being controlled by their phosphorylation status and by RanBP2 (Nup358), constituting the cytoplasmic filaments of NPC [300]. Two splicing factors, SRSF1 and 6, exihibit opposite effect on the progerin production by HGPS fibroblasts [301].…”

Section: Dna Replication Transcription Repair and Epigenetic Defectmentioning

confidence: 99%

Nuclear matrix, nuclear envelope and premature aging syndromes in a translational research perspective

Cau

Navarro

Harhouri

et al. 2014

Seminars in Cell & Developmental Biology

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Lamin A-related progeroid syndromes are genetically determined, extremely rare and severe. In the past ten years, our knowledge and perspectives for these diseases has widely progressed, through the progressive dissection of their pathophysiological mechanisms leading to precocious and accelerated aging, from the genes mutations discovery until therapeutic trials in affected children. A-type lamins are major actors in several structural and functional activities at the nuclear periphery, as they are major components of the nuclear lamina. However, while this is usually poorly considered, they also play a key role within the rest of the nucleoplasm, whose defects are related to cell senescence. Although nuclear shape and nuclear envelope deformities are obvious and visible events, nuclear matrix disorganization and abnormal composition certainly represent the most important causes of cell defects with dramatic pathological consequences. Therefore, lamin-associated diseases should be better referred as laminopathies instead of envelopathies, this later being too restrictive, considering neither the key structural and functional roles of soluble lamins in the entire nucleoplasm, nor the nuclear matrix contribution to the pathophysiology of lamin-associated disorders and in particular in defective lamin A processing-associated aging diseases. Based on both our understanding of pathophysiological mechanisms and the biological and clinical consequences of progeria and related diseases, therapeutic trials have been conducted in patients and were terminated less than 10 years after the gene discovery, a quite fast issue for a genetic disease. Pharmacological drugs have been repurposed and used to decrease the toxicity of the accumulated, unprocessed and truncated prelaminA in progeria. To date, none of them may be considered as a cure for progeria and these clinical strategies were essentially designed toward reducing a subset of the most dramatic and morbid features associated to progeria. New therapeutic strategies under study, in particular targeting the protein expression pathway at the mRNA level, have shown a remarkable efficacy both in vitro in cells and in vivo in mice models. Strategies intending to clear the toxic accumulated proteins from the nucleus are also under evaluation. However, although exceedingly rare, improving our knowledge of genetic progeroid syndromes and searching for innovative and efficient therapies in these syndromes is of paramount importance as, even before they can be used to save lives, they may significantly (i) expand the affected childrens' lifespan and preserve their quality of life; (ii) improve our understanding of aging-related disorders and other more common diseases; and (iii) expand our fundamental knowledge of physiological aging and its links with major physiological processes such as those involved in oncogenesis.

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“…It is noteworthy that, in FIV, loss of NUP358 isomerization correlates with lack of dependence on this co-factor for infection. Moreover FIV infection also occurs independently of TNPO3 (Figure 4d) [34,35], a nuclear transport factor that is involved in the same HIV-1 nuclear entry pathway as NUP358 [6,34] and whose subcellular localization has been shown to be affected by NUP358 depletion [36]. …”

Section: Resultsmentioning

confidence: 99%

HIV-1 capsid undergoes coupled binding and isomerization by the nuclear pore protein NUP358

et al. 2013

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BackgroundLentiviruses such as HIV-1 can be distinguished from other retroviruses by the cyclophilin A-binding loop in their capsid and their ability to infect non-dividing cells. Infection of non-dividing cells requires transport through the nuclear pore but how this is mediated is unknown.ResultsHere we present the crystal structure of the N-terminal capsid domain of HIV-1 in complex with the cyclophilin domain of nuclear pore protein NUP358. The structure reveals that HIV-1 is positioned to allow single-bond resonance stabilisation of exposed capsid residue P90. NMR exchange experiments demonstrate that NUP358 is an active isomerase, which efficiently catalyzes cis-trans isomerization of the HIV-1 capsid. In contrast, the distantly related feline lentivirus FIV can bind NUP358 but is neither isomerized by it nor requires it for infection.ConclusionIsomerization by NUP358 may be preserved by HIV-1 to target the nuclear pore and synchronize nuclear entry with capsid uncoating.

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The distribution of phosphorylated SR proteins and alternative splicing are regulated by RANBP2

Cited by 41 publications

References 74 publications

RNA Binding Motif Protein 48 is required for U12 splicing and maize endosperm differentiation

RNA Binding Motif Protein 48 is required for U12 splicing and maize endosperm differentiation

Nuclear matrix, nuclear envelope and premature aging syndromes in a translational research perspective

HIV-1 capsid undergoes coupled binding and isomerization by the nuclear pore protein NUP358

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