Browsing by Author "Fujita, Donald J."
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Item Open Access A search for binding partners of Golgin-67: potential interaction with guanine nucleotide dissociation inhibitor I(2003) Swancott, Abigail Jane Mary; Fujita, Donald J.Item Open Access Activation of src in human colon cancer cell lines(2006) Zhu, Shudong; Fujita, Donald J.Item Open Access Association of putative signal transduction intermediates with amino-terminal regulatory elements of the lymphocyte-specific protein tyrosine kinase p56lck(1993) Vogel, Lee B.; Fujita, Donald J.Item Open Access Characterization of an activated human pp60c-src mutant(1993) Bellagamba, Caterina; Fujita, Donald J.Item Open Access Characterization of tyrosine kinase-associated phosphatidylinositol-3 kinase(1993) Chan, Tung-On; Fujita, Donald J.Item Open Access Cloning and characterization of proteins antigenically related to Sam68 including a putative golgi protein that interacts with Src(1998) Raharjo, Eko Wargonyo; Fujita, Donald J.Item Open Access Development of SRC-GST fusion proteins for analysis of SRC functions(1996) Wang, Jing; Fujita, Donald J.Item Open Access Identification and characterization of a novel target of Src tyrosine kinase(2002) Jakymiw, Andrew George; Fujita, Donald J.Item Open Access Investigations into the Interaction between Src Kinase and Wnt Signaling(2009) Tang, Peter L.; Fujita, Donald J.Item Open Access Post-translational modifications regulating the activity of Sam68(2004) Babic, Ivan; Fujita, Donald J.Src-associated in mitosis 68 kDa (Sam68) is an RNA binding protein identified 10 years ago as a mitosis specific target for Src tyrosine kinase. It belongs to the signal transduction and activation of RNA metabolism (STAR) protein family. These proteins are thought to link signaling pathways with some aspect of RNA metabolism. Although the function of Sam68 is unknown it has been reported to play a role in several biological processes such as: viral replication, cell signaling, alternative pre-mRNA splicing, cell cycle regulation, and has been suggested to be a tumour suppressor and a transcriptional regulator. It has been demonstrated that the activity of Sam68 can be regulated by post-translational modifications such as tyrosine or serine/threonine phosphorylation. Tyrosine phosphorylation was shown to inhibit Sam68 binding to synthetic poly(U) RNA, and serine/threonine phosphorylation was shown to influence the ability of Sam68 to alter splice site selection. Since Sam68 is predominantly a nuclear protein there are several post-translational modifications common to nuclear proteins that have not yet been described for Sam68. For example, acetylation, sumoylation and ubquitination are three post-translational modifications described for numerous nuclear proteins. Here I report that Sam68 can be acetylated, and that acetylation positively regulates its binding to poly(U) RNA. As well, Sam68 is shown to be sumoylated. Conjugation with SUMO altered Sam68 subnuclear localization and its ability to act asItem Open Access Regulation of pp60c-src in melanocytes and melanoma cells(1994) O'Connor, Tracy J.; Fujita, Donald J.Item Open Access Src family kinase interactions with the vascular endothelial growth factor receptors(2003) Chou, Mary Trieu-Huy; Fujita, Donald J.Item Open Access Src Regulates the Activity of the ING1 Tumor Suppressor(PLoS, 2013-04-09) Yu, Lisa; Thakur, Satbir; Leong-Quong, Rebecca Y.Y.; Suzuki, Keiko; Pang, Andy; Bjorge, Jeffrey D.; Riabowol, Karl; Fujita, Donald J.; Fujita, Donald J.Item Open Access Src Regulation of von Hippel-Lindau Tumour Suppressor Protein(2009) Chou, Mary Trieu-Huy; Fujita, Donald J.Item Open Access Studies of mitogenesis induced by pp60v-src(1994) Berg, Randal Wayne; Fujita, Donald J.