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hnRNP M interacts with PSF and p54(nrb) and co-localizes within defined nuclear structures.
Exp Cell Res. 2010 Feb 01; 316(3):390-400.EC

Abstract

The abundant heterogeneous nuclear ribonucleoprotein M (hnRNP M) is able to associate with early spliceosomes and to influence splicing patterns of specific pre-mRNAs. Here, by a combination of immunoprecipitation and pull-down assays, we have identified PSF (polypyrimidine tract-binding protein-associated splicing factor) and p54(nrb), two highly related proteins involved in transcription and RNA processing, as new binding partners of hnRNP M. HnRNP M was found to co-localize with PSF within a subset of nuclear paraspeckles and to largely co-fractionate with PSF and p54(nrb) in biochemical nuclear matrix preparations. In cells transfected with an alternatively spliced preprotachykinin (PPT) minigene expression of hnRNP M promoted exon skipping while expression of PSF favours exon inclusion. The latter effect was reverted specifically by co-expressing the full length hnRNP M or a deletion mutant capable of interaction with PSF and p54(nrb). Together our data provide new insights and some functional implications on the hnRNP M network of interactions.

Authors+Show Affiliations

RNA Processing Laboratory, Institute of Biological Research and Biotechnology, National Hellenic Research Foundation, 48 Vas. Constantinou Avenue, 11635 Athens, Greece.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

19874820

Citation

Marko, Marija, et al. "HnRNP M Interacts With PSF and P54(nrb) and Co-localizes Within Defined Nuclear Structures." Experimental Cell Research, vol. 316, no. 3, 2010, pp. 390-400.
Marko M, Leichter M, Patrinou-Georgoula M, et al. HnRNP M interacts with PSF and p54(nrb) and co-localizes within defined nuclear structures. Exp Cell Res. 2010;316(3):390-400.
Marko, M., Leichter, M., Patrinou-Georgoula, M., & Guialis, A. (2010). HnRNP M interacts with PSF and p54(nrb) and co-localizes within defined nuclear structures. Experimental Cell Research, 316(3), 390-400. https://doi.org/10.1016/j.yexcr.2009.10.021
Marko M, et al. HnRNP M Interacts With PSF and P54(nrb) and Co-localizes Within Defined Nuclear Structures. Exp Cell Res. 2010 Feb 1;316(3):390-400. PubMed PMID: 19874820.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - hnRNP M interacts with PSF and p54(nrb) and co-localizes within defined nuclear structures. AU - Marko,Marija, AU - Leichter,Michael, AU - Patrinou-Georgoula,Meropi, AU - Guialis,Apostolia, Y1 - 2009/10/27/ PY - 2009/05/20/received PY - 2009/09/21/revised PY - 2009/10/21/accepted PY - 2009/10/31/entrez PY - 2009/10/31/pubmed PY - 2010/2/26/medline SP - 390 EP - 400 JF - Experimental cell research JO - Exp Cell Res VL - 316 IS - 3 N2 - The abundant heterogeneous nuclear ribonucleoprotein M (hnRNP M) is able to associate with early spliceosomes and to influence splicing patterns of specific pre-mRNAs. Here, by a combination of immunoprecipitation and pull-down assays, we have identified PSF (polypyrimidine tract-binding protein-associated splicing factor) and p54(nrb), two highly related proteins involved in transcription and RNA processing, as new binding partners of hnRNP M. HnRNP M was found to co-localize with PSF within a subset of nuclear paraspeckles and to largely co-fractionate with PSF and p54(nrb) in biochemical nuclear matrix preparations. In cells transfected with an alternatively spliced preprotachykinin (PPT) minigene expression of hnRNP M promoted exon skipping while expression of PSF favours exon inclusion. The latter effect was reverted specifically by co-expressing the full length hnRNP M or a deletion mutant capable of interaction with PSF and p54(nrb). Together our data provide new insights and some functional implications on the hnRNP M network of interactions. SN - 1090-2422 UR - https://www.unboundmedicine.com/medline/citation/19874820/hnRNP_M_interacts_with_PSF_and_p54_nrb__and_co_localizes_within_defined_nuclear_structures_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0014-4827(09)00461-3 DB - PRIME DP - Unbound Medicine ER -