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Heterogeneous nuclear ribonucleoprotein L

hnRNP L, heterogeneous nuclear ribonucleoprotein L
Heterogeneous nuclear RNAs (hnRNAs) which include mRNA precursors and mature mRNAs are associated with specific proteins to form heterogenous ribonucleoprotein (hnRNP) complexes. Heterogeneous nuclear ribonucleoprotein L is among the proteins that are stably associated with hnRNP complexes and along with other hnRNP proteins is likely to play a major role in the formation, packaging, processing, and function of mRNA. Heterogeneous nuclear ribonucleoprotein L is present in the nucleoplasm as part of the HNRP complex. HNRP proteins have also been identified outside of the nucleoplasm. Exchange of hnRNP for mRNA-binding proteins accompanies transport of mRNA from the nucleus to the cytoplasm. Since HNRP proteins have been shown to shuttle between the nucleus and the cytoplasm, it is possible that they also have cytoplasmic functions. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: fibrillin-1, CAN, PTB, V1a, CD45
Papers on hnRNP L
Antibodies specific for Epstein-Barr virus nuclear antigen-1 cross-react with human heterogeneous nuclear ribonucleoprotein L.
Zhao et al., Houston, United States. In Mol Immunol, Jan 2016
Anti-EBNA-1 consistently bound heterogeneous nuclear ribonucleoprotein L (HNRNPL).
Cyanotryptophans as Novel Fluorescent Probes for Studying Protein Conformational Changes and DNA-Protein Interaction.
Hecht et al., Tempe, United States. In Biochemistry, Jan 2016
Further, 6-CNTrp (A) was incorporated into two DNA binding proteins, including the Klenow fragment of DNA polymerase I and an RNA recognition motif (RRM2) of heterogeneous nuclear ribonucleoprotein L-like (hnRNP LL).
Global analysis of physical and functional RNA targets of hnRNP L reveals distinct sequence and epigenetic features of repressed and enhanced exons.
Lynch et al., Philadelphia, United States. In Rna, Dec 2015
HnRNP L is a ubiquitous splicing-regulatory protein that is critical for the development and function of mammalian T cells.
TDP-43 functions within a network of hnRNP proteins to inhibit the production of a truncated human SORT1 receptor.
Buratti et al., Jacksonville, United States. In Hum Mol Genet, Dec 2015
Here, we provide novel insight into the complexity of the RNA-binding protein network by demonstrating that the inclusion of exon 17b in the SORT1 mRNA, a pathologically relevant splicing event known to be regulated by TDP-43, is also considerably affected by additional RNA-binding proteins, such as hnRNP L, PTB/nPTB and hnRNP A1/A2.
Alteration of O-GlcNAcylation affects serine phosphorylation and regulates gene expression and activity of pyruvate kinase M2 in colorectal cancer cells.
Champattanachai et al., Bangkok, Thailand. In Oncol Rep, Oct 2015
Two-dimensional immunoblotting and mass spectrometric analysis showed that the levels of O-GlcNAc and serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1, were reduced in siOGT cells compared to siScramble cells.
The Signature of the Five-Stranded vRRM Fold Defined by Functional, Structural and Computational Analysis of the hnRNP L Protein.
Allain et al., Zürich, Switzerland. In J Mol Biol, Oct 2015
The heterogeneous nuclear ribonucleoprotein L (hnRNP L) is a highly abundant protein of 64 kDa comprising four RRM domains.
hnRNP L inhibits CD44 V10 exon splicing through interacting with its upstream intron.
Shen et al., Kwangju, South Korea. In Biochim Biophys Acta, Jun 2015
Here we show that increased expression of hnRNP L inhibits V10 exon splicing of CD44 pre-mRNA, whereas reduced expression of hnRNP L promotes V10 exon splicing.
Identification of DNA cleavage- and recombination-specific hnRNP cofactors for activation-induced cytidine deaminase.
Honjo et al., Kyoto, Japan. In Proc Natl Acad Sci U S A, Jun 2015
We found that hnRNP K deficiency inhibited DNA cleavage and thereby induced both CSR and SHM, whereas hnRNP L deficiency inhibited only CSR and somewhat enhanced SHM.
Proteomic identification of autoantibodies in sera from patients with ovarian cancer as possible diagnostic biomarkers.
Nagata et al., Tokyo, Japan. In Anticancer Res, Feb 2015
Elevated levels of autoantibodies against heterogeneous nuclear ribonucleoprotein L (hnRNPL) and a mitochondrial protein, dihydrolipoamide dehydrogenase (DLD), were detected in patients with CCC.
Identification of target antigens of antiendothelial cell antibodies against human brain microvascular endothelial cells in healthy subjects.
Inuzuka et al., Gifu, Japan. In Curr Neurovasc Res, 2014
We identified 7 proteins that corresponded to 8 of the 10 spots by mass spectrometry: 78-kDa glucose-regulated protein, dihydropyrimidinase-related protein 2, heterogeneous nuclear ribonucleoprotein L, vimentin, perilipin 3, alpha-enolase, and annexin A2.
Effects of oxygen on the antigenic landscape of prostate cancer cells.
Gomez et al., Jackson, United States. In Bmc Res Notes, 2014
We selected hypoxia-regulated HSP70 and hnRNP L and hypoxia-independent HSP60 and determined the frequency of plasma samples reacting with these molecules.
Optimization of immunostaining on flat-mounted human corneas.
He et al., Saint-Étienne, France. In Mol Vis, 2014
METHODS: The staining of four ubiquitous proteins, ZO-1, hnRNP L, actin, and histone H3, with clearly different subcellular localizations, was analyzed in ECs of organ-cultured corneas.
Improved binding site assignment by high-resolution mapping of RNA-protein interactions using iCLIP.
Kulozik et al., Heidelberg, Germany. In Nat Commun, 2014
Here we show that for several RBPs (eIF4A3, PTB, SRSF3, SRSF4 and hnRNP L), the start sites of iCLIP fragments show a fragment length-dependent broader distribution that can be shifted to positions upstream of the known RNA-binding site.
HnRNPL as a key factor in spermatogenesis: Lesson from functional proteomic studies of azoospermia patients with sertoli cell only syndrome.
Mao et al., Guangzhou, China. In J Proteomics, 2012
HnRNPL is a key factor involved in the spermatogenesis by functional proteomic studies of azoospermia patients with sertoli cell only syndrome.
Alternative splicing controlled by heterogeneous nuclear ribonucleoprotein L regulates development, proliferation, and migration of thymic pre-T cells.
Möröy et al., Montréal, Canada. In J Immunol, 2012
Constitutive deletion of splicing factor hnRNP L impedes early embryonic development of transgenic mice.
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.
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.
Repression of VEGFA by CA-rich element-binding microRNAs is modulated by hnRNP L.
Fox et al., Cleveland, United States. In Embo J, 2011
Hypoxia induces translocation of nuclear hnRNP L to the cytoplasm, which markedly increases hnRNP L binding to VEGFA mRNA thereby inhibiting miRNA activity.
NSP 5a3a's link to nuclear-cyto proteins B23 and hnRNP-L between normal and aberrant breast cell lines.
Giordano et al., Philadelphia, United States. In Cell Cycle, 2010
NSP 5a3a's novel interaction with B23 and ribonuclear protein hnRNP-L implicates NSP 5a3a in cellular processes such as ribosome biogenesis and rRNA transcription .
A stress-responsive RNA switch regulates VEGFA expression.
Fox et al., Cleveland, United States. In Nature, 2009
However, the VEGFA 3' UTR switch is metabolite-independent, and the conformational change is dictated by mutually exclusive, stimulus-dependent binding of proteins, namely, the IFN-gamma-activated inhibitor of translation complex and heterogeneous nuclear ribonucleoprotein L (HNRNPL, also known as hnRNP L).
Review: perinucleolar structures.
Huang, Chicago, United States. In J Struct Biol, 2000
In addition to the PNC and SNB, a perinucleolar structure immunolabeled with an antibody to hnRNP L will be discussed.
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