event generation of cancers. Indeed, a recent report suggested that KTMT attachment is more stable in cancer cells than in normal cells, arguing that persistence of aberrant KTMT attachment underlies the chromosome instability found in cancer cells. Thus, a defect in the error correction may have a causative function in generation of some type of cancers. To understand the 
steps towards sister KT bi-orientation, many pertinent questions remain to be answered. For example, PubMed ID:http://www.ncbi.nlm.nih.gov/pubmed/19828691 how do the Ndc80 complex, Dam1 complex and KNL1 cooperate to convert the lateral KTMT attachment to the end-on attachment What is the relative contribution of the error correction and KT geometry towards sister KT bi-orientation What processes do cells undergo during turnover of the KTMT attachment leading to the error correction; for example how is the old attachment removed and the new one established How does Aurora B/ Ipl1 promote turnover of the KTMT attachment through phosphorylation of KT substrates How does Mps1 contribute to the error correction; if Aurora B/Ipl1 is not the only target of Mps1, what are crucial substrates of Mps1 for the error correction The combined efforts in biochemistry, structural analyses, biophysics, genetics, cell biology and in silico study will advance research in this field. Acknowledgements I thank Lesley Clayton for helpful comments on the manuscript, and Yusuke Oku for making Conclusions and perspectives Establishing sister KT bi-orientation is a pivotal process ensuring equal segregation of the genetic information into daughter cells upon cell division. In particular, the tensiondependent error correction is a crucial MedChemExpress Sutezolid mechanism to secure sister KT bi-orientation. Sister KT bi-orientation and the error correction are not only fundamental for normal cell growth, Conflict of interest The author declares that he has no conflict of interest. Pre-mRNA splicing consists of a highly regulated cascade of events that are critical for gene expression in higher eukaryotic cells. This process has emerged as an important mechanism of genetic diversity, as about 9294% of human genes undergo alternative splicing, leading to the synthesis of various protein isoforms with different biological properties. SRSF2 belongs to the serine/arginine-rich Corresponding author. INSERM U823 Equipe 2, Institut Albert Bonniot, BP170, 38042 Grenoble Cedex 09, France. Tel.: 33 47 654 9476; Fax: 33 47 654 9413; E-mail: [email protected] Received: 18 May 2010; accepted: 17 November 2010; published online: 14 December 2010 protein family, one of the most important class of splicing regulators that has a prominent role in splice-site selection, in multiples steps of spliceosome assembly as well as in both constitutive and alternative splicing. All members of the SR protein family share a modular organization and contain one or two N-terminal RNA recognition motifs that interact with the premRNA, and influence substrate specificity, as well as a C-terminal SR sequence known as the RS domain that functions as a proteinprotein interaction module. Activity of SR proteins is highly regulated by extensive and reversible phosphorylation of serine residues inside RS domain. These phosphorylations modulate proteinprotein interactions within the spliceosome and can influence RNA-binding specificity, splicing activity and subcellular localization. To date, numerous kinases phosphorylating SR proteins have been identified. They include the SRPK and CLK/STY family k