Functional expression of cloned human splicing factor SF2: homology to rna-binding proteins, U1 70K, and drosophila splicing regulators

Cloning and characterization of two neural‐salient serine/arginine‐rich (NSSR) proteins involved in the regulation of alternative splicing in neurones

“…SR proteins are not only essential in general splicing but also in¯uence alternative splicing (Ge et al 1991;Krainer et al 1991;Wang et al 1996). Although alternative splicing occurs in a tissue-speci®c manner, little is known about tissue-speci®c SR proteins.…”

“…These are large RNA-protein complexes containing pre-mRNA and the U1, U2, U4/6, and U5 small nuclear ribonucleoprotein particles that associate with hnRNA, as well as a large number of accessory protein factors including the SR family of proteins (Kra Èmer 1996; Moore et al 1993;Rio 1993). The SR (serine/ arginine-rich) proteins comprise a family of splicing factors that are highly conserved in metazoa and have been studied extensively in vitro and in vivo (Ge et al 1991;Krainer et al 1991;Zahler et al 1993). It is thought that splicing assembly can be enhanced or suppressed by proteins that bind to cis-acting regulatory elements in pre-mRNA, and that the change in splicing form is determined by tissue-speci®c regulatory element binding proteins (trans-factors).…”

Differential expression of transcripts for the autoimmunity-related human dendritic cell immunoreceptor

“…ac.uk/asd-srv/wb.cgi), we found motifs for hnRNP.E1E2, hnRNP.I and hnRNP.K in this region, which suggest that this SNP might be involved in splicing repression, 11 and also SRp55 and ASF/SF2, which conversely suggest that the polymorphism rs2024301 is part of a splicing enhancer. [12][13][14] This does not give us conclusive information about causal variation, but build up a solid background for further vector-based analysis of the region is needed, for example, by using minigene constructs. 15,16 The difference between patients and healthy controls in expression is not as evident as the change associated with genotype.…”

Arginase II Contributes to the Ca 2+ /CaMKII/eNOS Axis by Regulating Ca 2+ Concentration Between the Cytosol and Mitochondria in a p32‐Dependent Manner

“…p32, also known as HABP1 (hyaluronan‐binding protein 1), is a receptor for gC1qR (globular head domains complement 1q), or C1qbp (complement 1q‐binding protein), and has been recognized as a pre‐mRNA splicing factor SF2‐binding protein in the nucleus23 and a receptor interacting with the complement component C1q on the cell surface 24. Although p32 can be existed in multicellular compartments, it is predominantly targeted to mitochondria because of the mitochondrial targeting sequence contained in the 73N‐terminal amino acids 25.…”