hnRNP K: One protein multiple processes
Article first published online: 24 MAY 2004
Copyright © 2004 Wiley Periodicals, Inc.
Volume 26, Issue 6, pages 629–638, June 2004
How to Cite
Bomsztyk, K., Denisenko, O. and Ostrowski, J. (2004), hnRNP K: One protein multiple processes. Bioessays, 26: 629–638. doi: 10.1002/bies.20048
- Issue published online: 24 MAY 2004
- Article first published online: 24 MAY 2004
- NIH GM45134, DK45978 and Fogarty International Research Collaboration Award (FIRCA) TW05685, the Juvenile Diabetes Research Foundation 1-2002-80, the Northwest Kidney Foundation (K.B.)
- Polish Committee for Scientific Research (J.O.)
Since its original identification as a component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complex, K protein has been found not only in the nucleus but also in the cytoplasm and mitochondria and is implicated in chromatin remodeling, transcription, splicing and translation processes. K protein contains multiple modules that, on one hand, bind kinases while, on the other hand, recruit chromatin, transcription, splicing and translation factors. Moreover, the K- protein-mediated interactions are regulated by signaling cascades. These observations are consistent with K protein acting as a docking platform to integrate signaling cascades by facilitating cross-talk between kinases and factors that mediate nucleic-acid-directed processes. Comparison of K across species reveals that it is an essential factor in metazoans, but not in yeast. Although some of the K protein interactions and functions are conserved in eukaryotes from yeast to man, the mammalian protein seems to play a wider role. The greater diversity of mammalian K protein interactions and function may reflect gain of novel docking sites and expansion evolutionary of gene expression networks. BioEssays 26:629–638, 2004. © 2004 Wiley Periodicals, Inc.