Characterization of alpha-catulin, a new dystrophin-associated protein.
Published: 2004
Language: eng
Number of pages: 136
Description: This thesis further characterized alpha-catulin by investigating its interacting proteins via a yeast two-hybrid screen. Utrophin and talin were selected and their interactions with alpha-catulin were further investigated via non-yeast methods. Hydrophilic and hydrophobic C-terminal dystrophin isoforms were found to be differentially localized in the heart with alpha-catulin, co-localizing with the latter. Together, these findings support the hypothesis that the dystrophin hydrophilic and hydrophobic C-termini are performing unique functions in different tissues.The dystrophin gene gives rise to a diverse family of transcripts generated through alternative promoter usage and alternative splicing. The most common splicing event involves exon 78 and changes the C-terminus of the resultant protein from a hydrophilic C-terminus to a hydrophobic C-terminus. Recently in our lab it has been discovered that the alternative splicing event excluding exon 78 creates a new protein-binding site in dystrophin that interacts with alpha-catulin, a relatively uncharacterized protein.
Notes: Adviser:  Peter Ray.

Thesis (M.Sc.)--University of Toronto, 2004.

Electronic version licensed for access by U. of T. users.

Source: Masters Abstracts International, Volume: 43-03, page: 0776.

MICR copy on microfiche (2 microfiches).