Repository logo
  • English
  • Català
  • Čeština
  • Deutsch
  • Español
  • Français
  • Gàidhlig
  • Latviešu
  • Magyar
  • Nederlands
  • Polski
  • Português
  • Português do Brasil
  • Suomi
  • Svenska
  • Türkçe
  • Қазақ
  • বাংলা
  • हिंदी
  • Ελληνικά
  • Yкраї́нська
  • Log In
    or
    New user? Click here to register.Have you forgotten your password?
Repository logo
  • PRISM

  • Communities & Collections
  • All of PRISM
  • English
  • Català
  • Čeština
  • Deutsch
  • Español
  • Français
  • Gàidhlig
  • Latviešu
  • Magyar
  • Nederlands
  • Polski
  • Português
  • Português do Brasil
  • Suomi
  • Svenska
  • Türkçe
  • Қазақ
  • বাংলা
  • हिंदी
  • Ελληνικά
  • Yкраї́нська
  • Log In
    or
    New user? Click here to register.Have you forgotten your password?
  1. Home
  2. Browse by Author

Browsing by Author "Babic, Ivan"

Now showing 1 - 2 of 2
Results Per Page
Sort Options
  • Loading...
    Thumbnail Image
    Item
    Open Access
    Elevated expression of wild type and mutated forms of a brassica napas acetolactate synthase gene for herbicide resistance in b. napus
    (1991) Babic, Ivan; Moloney, Maurice M.
  • Loading...
    Thumbnail Image
    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 as

Libraries & Cultural Resources

  • Contact us
  • 403.220.8895
Start Something.
  • Digital Privacy Statement
  • Privacy Policy
  • Website feedback

University of Calgary
2500 University Drive NW
Calgary Alberta T2N 1N4
CANADA

Copyright © 2023

The University of Calgary acknowledges the traditional territories of the people of the Treaty 7 region in Southern Alberta, which includes the Blackfoot Confederacy (comprised of the Siksika, Piikani, and Kainai First Nations), as well as the Tsuut’ina First Nation, and the Stoney Nakoda (including the Chiniki, Bearspaw and Wesley First Nations). The City of Calgary is also home to Metis Nation of Alberta, Region 3. The University of Calgary acknowledges the impact of colonization on Indigenous peoples in Canada and is committed to our collective journey towards reconciliation to create a welcome and inclusive campus that encourages Indigenous ways of knowing, doing, connecting and being.