The RGG Domain in hnRNP A2 Affects Subcellular Localization

Nichols, Ralph C.; Wang, Xiao Wei; Tang, Jie; Hamilton, Byron B.; High, Frances A.; Herschman, Harvey R.; Rigby, William F.C.

doi:10.1006/excr.2000.4827

Cited by 160 publications

(155 citation statements)

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“…Protein arginine methyltransferase 1 represents the prevalent protein methyltransferase in human cells. The major targets of PRMT1 include components of the hnRNPs (Nichols et al, 2000), histone H4 (Wang et al, 2001) and peroxisome proliferator-activated receptor g coactivator 1a (Teyssier et al, 2005). It is known for a long time now that alterations in the expression pattern of certain genes are strongly correlated with cancer incidence.…”

Section: Discussionmentioning

confidence: 99%

The PRMT1 gene expression pattern in colon cancer

et al. 2008

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The methylation of arginine has been implicated in many cellular processes, such as regulation of transcription, mRNA splicing, RNA metabolism and transport. The enzymes responsible for this modification are the protein arginine methyltransferases. The most abundant methyltransferase in human cells is protein arginine methyltransferase 1. Methylation processes appear to interfere in the emergence of several diseases, including cancer. During our study, we examined the expression pattern of protein arginine methyltransferase 1 gene in colon cancer patients. The emerging results showed that the expression of one of the gene variants is associated with statistical significant probability to clinical and histological parameters, such as nodal status and stage. This is a first attempt to acquire an insight on the possible relation of the expression pattern of protein arginine methyltransferase 1 and colon cancer progression.

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Section: Discussionmentioning

confidence: 99%

The PRMT1 gene expression pattern in colon cancer

et al. 2008

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“…There were, however, significant differences in site abundance between NSCLC serum samples compared with AML or BC, including heterogeneous nuclear ribonucleoproteins, well-studied RNA processing proteins involved in posttranscriptional modification of pre-mRNA (42). Methylation of hnRNP family members containing the RGG motif promotes import into the nucleus (43). Therefore, changes in the levels of identified arginine methylation level in hnRNPs such as Arg291 of hnRNP A0, Arg206 of hnRNP A1, Arg203 of hnRNP A2/B1, and Arg272 of hnRNP D0 may help estimate their nucleo-cytoplasmic shuttling as well as posttranscriptional regulation in different cancers.…”

Section: Fig 2 Functional Classification Of Functions Of Proteins Imentioning

confidence: 99%

Quantitative Profiling of Post-translational Modifications by Immunoaffinity Enrichment and LC-MS/MS in Cancer Serum without Immunodepletion

Ren

Jia

et al. 2016

Molecular & Cellular Proteomics

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Biomarker identification is a key step for illustration of disease mechanisms, drug development, and diagnostics. Diagnostics research has focused on identifying biomarkers from viable biofluids, including serum/plasma, saliva, cerebrospinal fluid, and urine. Due to ease of collection and richness in proteins and metabolites, serum/plasma has been the preferred choice for diagnostic studies (1-3). Advancement of mass-spectrometry-based proteomic technologies has allowed identification and quantification of thousands of proteins in serum/plasma samples. Typically, these methods combine isotopic labeling, offline fractionation, and LC-MS/MS analysis. Facilitated by high-throughput proteomics analysis, researchers have collected vast amounts of comparative information about protein abundance in serum/plasma of patients of various types of diseases that accelerated the identification of potential biomarkers (4).To date, the majority of serum/plasma proteomic work has been conducted to analyze total protein level abundance, with only a few studies to analyze posttranslational modifications (PTMs) 1 , usually glycosylation (5, 6). As one of the most important mechanisms for regulating protein function, PTMs, including phosphorylation, acetylation, ubiquitination, and methylation, have been identified and validated as critical for signaling transduction, protein degradation, and transcriptional regulation (7,8). Currently, there exists very limited data about PTMs in serum/plasma beyond glycosylation. The abundant serum protein albumin has long been known to be acetylated by aspirin, and this reaction can occur in vitro without the presence of any acetyltransferase (9). Fibrinogen, another abundant serum protein, is also acetylated by aspirin both in vivo and in vitro (10, 11). These previous findings and the known importance of PTMs in cellular signaling provided the impetus for a large-scale survey of PTMs other than glycosylation by immunoaffinity enrichment of PTM-containing peptides.One challenge for proteomic analysis of serum/plasma is the broad dynamic range of the serum/plasma proteome (12), including a high percentage of the total protein content of serum/plasma represented by only 12 proteins. This limitation can be partially overcome by immunodepletion of abundant proteins prior to enzymatic digestion (4, 13), however, generation of the large quantities of materials necessary for PTM enrichment with an immunodepletion workflow could be cost prohibitive. It was therefore of interest to develop a PTM

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“…Mouse monoclonal antibody to hnRNP A2 (EF67) (used at 1:400 dilution) was a generous gift from Dr. William Rigby (Dartmouth Medical School, Lebanon, NH) (Nichols et al, 2000). A rabbit antibody produced against a fragment of TOG encompassing residues 829-1564 and 1623-1957 ( Figure 1A) was a generous gift from Dr. Christian Larroque (Institut National de la Santé et de la Recherche Médicale, Montpellier, France) (Charrasse et al, 1998).…”

Section: Immunofluorescence Microinjection and Image Acquisition Anmentioning

confidence: 99%

The Microtubule-associated Protein Tumor Overexpressed Gene Binds to the RNA Trafficking Protein Heterogeneous Nuclear Ribonucleoprotein A2

Kosturko

Maggipinto

D'Sa

et al. 2005

MBoC

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In neural cells, such as oligodendrocytes and neurons, transport of certain RNAs along microtubules is mediated by the cis-acting heterogeneous nuclear ribonucleoprotein A2 response element (A2RE) trafficking element and the cognate trans-acting heterogeneous nuclear ribonucleoprotein (hnRNP) A2 trafficking factor. Using a yeast two-hybrid screen, we have identified a microtubule-associated protein, tumor overexpressed gene (TOG)2, as an hnRNP A2 binding partner. The C-terminal third of TOG2 is sufficient for hnRNP A2 binding. TOG2, the large protein isoform of TOG, is the only isoform detected in oligodendrocytes in culture. TOG coimmunoprecipitates with hnRNP A2 present in the cytoskeleton (CSK) fraction of neural cells, and both coprecipitate with microtubule stabilized pellets. Staining with anti-TOG reveals puncta that are localized in proximity to microtubules, often at the plus ends. TOG is colocalized with hnRNP A2 and A2RE-mRNA in trafficking granules that remain associated with CSK-insoluble tissue. These data suggest that TOG mediates the association of hnRNP A2-positive granules with microtubules during transport and/or localization. INTRODUCTIONThe heterogeneous nuclear ribonucleoprotein (hnRNP) A2 is implicated in RNA processing, RNA transport, and translation regulation (Dreyfuss et al., 1993;Siomi and Dreyfuss, 1995;Hamilton et al., 1999;Kwon et al., 1999). HnRNP A2 binds to a specific cis-acting element, hnRNP A2 response element (A2RE), found in several dendritically localized mRNAs Munro et al., 1999). This interaction is necessary for transport of A2RE-mRNAs to the periphery of neural cells (Munro et al., 1999;Shan et al., 2003).A2RE-mRNAs, hnRNP A2, and other components form complexes that look by light microscopy like granules that are transported to the cell periphery by a microtubule-and kinesin-based mechanism. In cultured oligodendrocytes and neurons, granules containing A2RE-mRNAs and hnRNP A2 are associated with the cytoskeleton (CSK) . HnRNP A2 and some A2RE-mRNAs copurify with the CSK from rat brain (Hoek et al., 1998;Boccaccio et al., 1999).To identify molecular partners of hnRNP A2, we performed yeast two-hybrid analysis. One of the components identified is the tumor overexpressed gene (TOG) protein, a microtubule-associated protein (MAP) ubiquitously expressed in human tissues. TOG is a single copy gene that generates two mRNA splice variants (Nagase et al., 1995;Charrasse et al., 1998) encoding proteins that differ by a 60-aa insert near the C terminus. In dividing cells, TOG localizes with centrosome and spindle microtubules and may be necessary for microtubule rearrangements and spindle assembly (Charrasse et al., 1998;Lee et al., 2001). Orthologues of colonic and hepatic tumor overexpressed gene (ch-TOG) (Homo sapiens), Dis1p, Stu2p, XMAP215, ZYG-9, and mini spindles, in fission yeast, budding yeast, Xenopus laevis, Caenorhabditis elegans, and Drosophila melanogaster, respectively, have similar functions. TOG and its orthologues all contain multiple HEAT repeats that may serv...

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The RGG Domain in hnRNP A2 Affects Subcellular Localization

Cited by 160 publications

References 54 publications

The PRMT1 gene expression pattern in colon cancer

The PRMT1 gene expression pattern in colon cancer

Quantitative Profiling of Post-translational Modifications by Immunoaffinity Enrichment and LC-MS/MS in Cancer Serum without Immunodepletion

The Microtubule-associated Protein Tumor Overexpressed Gene Binds to the RNA Trafficking Protein Heterogeneous Nuclear Ribonucleoprotein A2

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