Literature DB >> 8558240

The onconeural antigen Nova-1 is a neuron-specific RNA-binding protein, the activity of which is inhibited by paraneoplastic antibodies.

R J Buckanovich1, Y Y Yang, R B Darnell.   

Abstract

Nova-1, a protein expressed in tumors and neurons, is a target antigen in a human paraneoplastic motor disorder [paraneoplastic opsoclonus-myoclonus ataxia (POMA)]. We evaluated the relationship between the function of Nova-1 and its role as a disease antigen. We show that Nova-1 is a neuron-specific RNA-binding protein with sequence and functional similarities to FMR-1. Nova-1 mRNA is restricted to the subcortical nervous system, and the protein binds to RNA with high affinity. Nova-1 KH domains mediate this RNA binding, and point mutations within them abrogate binding. POMA disease antisera (6/6) recognize the third KH domain but not an inactive point mutant, and affinity-purified antibody blocks Nova-1 RNA binding. Thus, a cardinal feature of POMA is the production of antibodies that inhibit Nova-1-RNA interactions, suggesting such inhibition may cause the neurological disease.

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Year:  1996        PMID: 8558240      PMCID: PMC6578795     

Source DB:  PubMed          Journal:  J Neurosci        ISSN: 0270-6474            Impact factor:   6.167


  73 in total

1.  The tetranucleotide UCAY directs the specific recognition of RNA by the Nova K-homology 3 domain.

Authors:  K B Jensen; K Musunuru; H A Lewis; S K Burley; R B Darnell
Journal:  Proc Natl Acad Sci U S A       Date:  2000-05-23       Impact factor: 11.205

2.  Determination and augmentation of RNA sequence specificity of the Nova K-homology domains.

Authors:  Kiran Musunuru; Robert B Darnell
Journal:  Nucleic Acids Res       Date:  2004-09-14       Impact factor: 16.971

3.  Nova autoregulation reveals dual functions in neuronal splicing.

Authors:  B Kate Dredge; Giovanni Stefani; Caitlin C Engelhard; Robert B Darnell
Journal:  EMBO J       Date:  2005-03-31       Impact factor: 11.598

4.  A nuclear function of Hu proteins as neuron-specific alternative RNA processing regulators.

Authors:  Hui Zhu; Robert A Hasman; Victoria A Barron; Guangbin Luo; Hua Lou
Journal:  Mol Biol Cell       Date:  2006-10-11       Impact factor: 4.138

Review 5.  RNA protein interaction in neurons.

Authors:  Robert B Darnell
Journal:  Annu Rev Neurosci       Date:  2013-05-20       Impact factor: 12.449

6.  Genome analysis: RNA recognition motif (RRM) and K homology (KH) domain RNA-binding proteins from the flowering plant Arabidopsis thaliana.

Authors:  Zdravko J Lorković; Andrea Barta
Journal:  Nucleic Acids Res       Date:  2002-02-01       Impact factor: 16.971

7.  A brain-enriched polypyrimidine tract-binding protein antagonizes the ability of Nova to regulate neuron-specific alternative splicing.

Authors:  A D Polydorides; H J Okano; Y Y Yang; G Stefani; R B Darnell
Journal:  Proc Natl Acad Sci U S A       Date:  2000-06-06       Impact factor: 11.205

8.  In vitro genetic analysis of the RNA binding site of vigilin, a multi-KH-domain protein.

Authors:  H Kanamori; R E Dodson; D J Shapiro
Journal:  Mol Cell Biol       Date:  1998-07       Impact factor: 4.272

Review 9.  Faulty RNA splicing: consequences and therapeutic opportunities in brain and muscle disorders.

Authors:  Vittoria Pagliarini; Piergiorgio La Rosa; Claudio Sette
Journal:  Hum Genet       Date:  2017-04-22       Impact factor: 4.132

Review 10.  Onconeural antigens and the paraneoplastic neurologic disorders: at the intersection of cancer, immunity, and the brain.

Authors:  R B Darnell
Journal:  Proc Natl Acad Sci U S A       Date:  1996-05-14       Impact factor: 11.205

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