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Heterogeneous nuclear ribonucleoprotein M

hnRNP M, N-acetylglucosamine receptor, heterogeneous nuclear ribonucleoprotein M, NAGR1
This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene has three repeats of quasi-RRM domains that bind to RNAs. This protein also constitutes a monomer of the N-acetylglucosamine-specific receptor which is postulated to trigger selective recycling of immature GlcNAc-bearing thyroglobulin molecules. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2011] (from NCBI)
Top mentioned proteins: CAN, ACID, fibrillin-1, CIs, STEP
Papers on hnRNP M
Heterogeneous Nuclear Ribonucleoprotein M Facilitates Enterovirus Infection.
New
Jan et al., In J Virol, Jul 2015
Here, using a proteomics-based approach known as TAILS to identify protease-generated neo-N-terminal peptides, we identify a novel target of the poliovirus 3C proteinase, the heterogeneous nuclear ribonucleoproteinM(hnRNP M), a nucleocytoplasmic shuttling RNA-binding protein that is primarily known for its role in pre-mRNA splicing.
In vitro identification of nonalcoholic fatty liver disease-related protein hnRNPM.
New
Hori et al., Hiroshima, Japan. In World J Gastroenterol, Mar 2015
The heterogeneous nuclear ribonucleoprotein M (hnRNPM), which plays an important role in regulating gene expression by processing heterogeneous nuclear RNAs to form mature mRNAs, was identified as a modified protein using MALDI-TOF-MS.
Targeted gene delivery via N-acetylglucosamine receptor mediated endocytosis.
Cho et al., In J Nanosci Nanotechnol, 2014
Receptor-mediated endocytosis is a promising approach of gene delivery into the target cells via receptor-ligand interaction.
The RNA-binding protein Rumpelstiltskin antagonizes gypsy chromatin insulator function in a tissue-specific manner.
Lei et al., Bethesda, United States. In J Cell Sci, 2014
Here, we identify the Drosophila hnRNP M homolog Rumpelstiltskin (Rump) as an antagonist of gypsy chromatin insulator enhancer-blocking and barrier activities.
Cell type-restricted activity of hnRNPM promotes breast cancer metastasis via regulating alternative splicing.
Cheng et al., Chicago, United States. In Genes Dev, 2014
We show that the RNA-binding protein heterogeneous nuclear ribonucleoprotein M (hnRNPM) promotes breast cancer metastasis by activating the switch of alternative splicing that occurs during epithelial-mesenchymal transition (EMT).
The transcription-splicing protein NonO/p54nrb and three NonO-interacting proteins bind to distal enhancer region and augment rhodopsin expression.
Swaroop et al., Bethesda, United States. In Hum Mol Genet, 2014
We validate the binding of NonO (p54(nrb)), a protein implicated in coupling transcription to splicing, and three NonO-interacting proteins-hnRNP M, Ywhaz and Ppp1ca.
Identification of HnRNP M as a novel biomarker for colorectal carcinoma by quantitative proteomics.
Liu et al., Changsha, China. In Am J Physiol Gastrointest Liver Physiol, 2014
The function of heterogeneous nuclear ribonucleoprotein M (HnRNP M) during the proliferation, invasion, and metastasis of CRC cells in vitro was evaluated.
hnRNP M facilitates exon 7 inclusion of SMN2 pre-mRNA in spinal muscular atrophy by targeting an enhancer on exon 7.
Shen et al., Kwangju, South Korea. In Biochim Biophys Acta, 2013
Here we show that hnRNP M, a member of hnRNP protein family, when knocked down, promotes exon 7 skipping of both SMN2 and SMN1 pre-mRNA.
Selective interactions of hnRNP M isoforms with the TET proteins TAF15 and TLS/FUS.
Guialis et al., Köln, Germany. In Mol Biol Rep, 2013
Finally, we show partial co-localization of TAF15 and TLS/FUS with hnRNP M proteins in HeLa nuclei, supporting the biochemically obtained data.
Magnetic fractionation and proteomic dissection of cellular organelles occupied by the late replication complexes of Semliki Forest virus.
Merits et al., Tartu, Estonia. In J Virol, 2013
These host components included the RNA-binding proteins PCBP1, hnRNP M, hnRNP C, and hnRNP K, which were shown to colocalize with the viral replicase.
Identification of potential mediators of retinotopic mapping: a comparative proteomic analysis of optic nerve from WT and Phr1 retinal knockout mice.
Culican et al., Saint Louis, United States. In J Proteome Res, 2012
One of these, heterogeneous nuclear ribonucleoprotein M (hnRNP-M), regulates antero-posterior patterning in invertebrates and can function as a cell surface adhesion receptor in vertebrates.
Engagement of heterogeneous nuclear ribonucleoprotein M with listeriolysin O induces type I interferon expression and restricts Listeria monocytogenes growth in host cells.
Zheng et al., Beijing, China. In Immunobiology, 2012
Using pull-down assay, mass spectrometry analysis and immunoprecipitation approaches, we found that LLO interacted with heterogeneous nuclear ribonucleoprotein M (hnRNPM), a member of RNA splicing complex apparatus, and the binding domain of LLO for hnRNP M was located between amino acids 26 and 176.
Hexapeptide fragment of carcinoembryonic antigen which acts as an agonist of heterogeneous ribonucleoprotein M.
Lovas et al., Omaha, United States. In J Pept Sci, 2012
CEA binds to the heterogeneous ribonucleoprotein M (hnRNP M) which acts as a cell surface receptor in Kupffer cells.
Carcinoembryonic antigen (CEA) and its receptor hnRNP M are mediators of metastasis and the inflammatory response in the liver.
Review
Bajenova et al., Omaha, United States. In Clin Exp Metastasis, 2011
CEA acts in the liver through its interaction with its receptor (CEAR), a protein that is related to the hnRNP M family of RNA binding proteins.
Mechanistic control of carcinoembryonic antigen-related cell adhesion molecule-1 (CEACAM1) splice isoforms by the heterogeneous nuclear ribonuclear proteins hnRNP L, hnRNP A1, and hnRNP M.
GeneRIF
Gaur et al., Duarte, United States. In J Biol Chem, 2011
Mechanistic control of carcinoembryonic antigen-related cell adhesion molecule-1 (CEACAM1) splice isoforms by the heterogeneous nuclear ribonuclear proteins hnRNP L, hnRNP A1, and hnRNP M.
Direct interaction between hnRNP-M and CDC5L/PLRG1 proteins affects alternative splice site choice.
GeneRIF
Lamond et al., Dundee, United Kingdom. In Embo Rep, 2010
A central region in hnRNP-M is required for interaction with CDC5L/PLRG1.
hnRNP M interacts with PSF and p54(nrb) and co-localizes within defined nuclear structures.
GeneRIF
Guialis et al., Athens, Greece. In Exp Cell Res, 2010
PSF (polypyrimidine tract-binding protein-associated splicing factor) and p54(nrb), two highly related proteins involved in transcription and RNA processing, are identified as new binding partners of hnRNP M.
cis-acting sequences and trans-acting factors in the localization of mRNA for mitochondrial ribosomal proteins.
GeneRIF
Russo et al., Napoli, Italy. In Biochim Biophys Acta, 2008
mitochondrial ribosomal protein S12 3'-UTR interacts specifically with TRAP1 (tumor necrosis factor receptor-associated protein1), hnRNPM4 (heterogeneous nuclear ribonucleoprotein M4), Hsp70 and Hsp60 (heat shock proteins 70 and 60), and alpha-tubulin
Role of thyroglobulin endocytic pathways in the control of thyroid hormone release.
Review
McCluskey et al., United States. In Am J Physiol Cell Physiol, 2000
A thyroid asialoglycoprotein receptor may internalize and recycle immature forms of Tg back to the colloid, a function also attributed to an as yet unidentified N-acetylglucosamine receptor.
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