S1‐1/RBM10: Multiplicity and cooperativity of nuclear localisation domains

Xiao, Sheng-Jun; Ly, Wang; Kimura, Michio; Kojima, Hiroyuki; Kunimoto, Hiroyuki; Nishiumi, Fumiko; Yamamoto, Naoki; Nishio, Koji; Fujimoto, Shuhei; Kato, Takayuki; Kitagawa, Seiichi; Yamane, Hideo; Nakajima, Kōichi; Inoue, Akira

doi:10.1111/boc.201200068

Cited by 17 publications

(34 citation statements)

References 50 publications

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“…Overexpression (OE) of RBM10 -EGFP WT in HEK293 cells also increased exon skipping in five known RBM10 target genes (Supplementary Fig. S2), in agreement with previous studies263637. These observations confirm that fusing EGFP to the C-terminus of RBM10 does not interfere with its function, and thus demonstrate that RBM10 fusion proteins can be used in functional assays.…”

Section: Resultssupporting

confidence: 90%

Functional analysis reveals that RBM10 mutations contribute to lung adenocarcinoma pathogenesis by deregulating splicing

Zhao

Sun

Huang

et al. 2017

Sci Rep

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RBM10 is an RNA splicing regulator that is frequently mutated in lung adenocarcinoma (LUAD) and has recently been proposed to be a cancer gene. How RBM10 mutations observed in LUAD affect its normal functions, however, remains largely unknown. Here integrative analysis of RBM10 mutation and RNA expression data revealed that LUAD-associated RBM10 mutations exhibit a mutational spectrum similar to that of tumor suppressor genes. In addition, this analysis showed that RBM10 mutations identified in LUAD patients lacking canonical oncogenes are associated with significantly reduced RBM10 expression. To systematically investigate RBM10 mutations, we developed an experimental pipeline for elucidating their functional effects. Among six representative LUAD-associated RBM10 mutations, one nonsense and one frameshift mutation caused loss-of-function as expected, whereas four missense mutations differentially affected RBM10-mediated splicing. Importantly, changes in proliferation rates of LUAD-derived cells caused by these RBM10 missense mutants correlated with alterations in RNA splicing of RBM10 target genes. Together, our data implies that RBM10 mutations contribute to LUAD pathogenesis, at least in large part, by deregulating splicing. The methods described in this study should be useful for analyzing mutations in additional cancer-associated RNA splicing regulators.

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Section: Resultssupporting

confidence: 90%

Functional analysis reveals that RBM10 mutations contribute to lung adenocarcinoma pathogenesis by deregulating splicing

Zhao

Sun

Huang

et al. 2017

Sci Rep

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“…Together, our present results indicate that a notable cytoplasmic presence of RBM10 occurs not only in hepatocellular carcinoma cells and cirrhotic hepatocytes, 18 but also in cells of complete hydatidiform mole. This suggests that a cytoplasmic occurrence is a sign or characteristic of disease, involving disruption of normal cell physiology.…”

Section: Discussionsupporting

confidence: 73%

“…9 A 58 kDa protein was previously detected in the human promyelocytic leukemia cell line HL-60, but its corresponding mRNA was not found and the protein was considered to be a proteolytic product of RBM10. 18 The cytoplasmic 50 kDa protein detected in the present study is also considered to be a proteolytic product of RBM10, as the upper 58 kDa band rapidly diminished during prolonged sample-handling time such that the 50 kDa polypeptide accumulated in the cytoplasmic fraction (data not shown).…”

Section: Discussionmentioning

confidence: 56%

RBM10 in complete hydatidiform mole: cytoplasmic occurrence of its 50 kDa polypeptide

Inoue

Honda

Inoue

et al. 2013

Int J Reprod Contracept Obstet Gynecol

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Background: RNA-binding motif protein 10 (RBM10), originally identified as S1-1 protein, is a nuclear protein with likely functions in transcription and RNA splicing. The RBM10 gene maps to the X chromosome and, in female cells, is inactivated in one of the two X chromosomes near the boundary with genes escaping inactivation. This study investigated the occurrence of the RBM10 gene product in complete hydatidiform mole, which is composed of cells with paternal diploid chromosomes (46, XX). Methods: Deparaffinized normal chorion or complete hydatidiform mole tissues were hybridized with a fluorescein-conjugated RBM10 gene probe in fluorescent in situ hybridization (FISH) analysis. Immunohistochemistry and immunoelectron microscopy of the tissues were performed using an anti-RBM10 antiserum. Proteins from complete hydatidiform mole tissues and those separated by anti-RBM10-linked affinity chromatography were also examined by western blotting. Results: As expected, the RBM10 gene was detected by FISH as double spots in the nuclei of complete hydatidiform mole cells. Immunohistochemistry revealed a nuclear presence of RBM10 in normal chorion and complete hydatidiform moles, and a notable cytoplasmic presence in complete hydatidiform moles. Western blotting and immunoaffinity chromatography revealed that a 50 kDa protein was predominantly found in the cytosolic fraction of complete hydatidiform moles. Conclusions: A 50 kDa protein with common antigenicity to RBM10 was found in the cytoplasm of complete hydatidiform mole cells, and could represent one of the characteristics of the disease. [Int J Reprod Contracept Obstet Gynecol 2013; 2(2.000): 114-118

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“…, whereas three NLSs were found in mammalian 5-lipoxygenase, human S1-1/RBM10, human Dot1a, and human Tra2␤ (24)(25)(26)(27). As far as we know, there is no reported example of a nuclear protein with more than three NLSs.…”

mentioning

confidence: 96%

Multiple Nuclear Localization Signals Mediate Nuclear Localization of the GATA Transcription Factor AreA

et al. 2014

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S1‐1/RBM10: Multiplicity and cooperativity of nuclear localisation domains

Cited by 17 publications

References 50 publications

Functional analysis reveals that RBM10 mutations contribute to lung adenocarcinoma pathogenesis by deregulating splicing

Functional analysis reveals that RBM10 mutations contribute to lung adenocarcinoma pathogenesis by deregulating splicing

RBM10 in complete hydatidiform mole: cytoplasmic occurrence of its 50 kDa polypeptide

Multiple Nuclear Localization Signals Mediate Nuclear Localization of the GATA Transcription Factor AreA

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