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Characterisation of the Non-Canonical Translation Initiation Factor eIF4E-3 as a Merlin Interacting Protein in Drosophila melanogaster

  • Author / Creator
    Arnold, Kirsten J
  • Merlin is a tumour suppressor protein, the loss of which is linked to the inherited nervous system tumour syndrome Neurofibromatosis type 2 as well as sporadic tumour development. It is related to the ERM (ezrin-radixin-moesin) protein family, which is involved in linking the cytoskeleton to membrane associated proteins and thereby coordinating processes such as cell shape and polarity. However, Merlin’s activity as a tumour suppressor is not clearly defined, nor is it clear why tumours form primarily in the nervous system although Merlin is broadly expressed. Merlin has numerous interacting partners, and a possible explanation for nervous system specific tumour development is that one or more Merlin interacting proteins modifies its tumour suppressor activity in these cell types. In Drosophila melanogaster, a non-canonical translation initiation factor eIF4E 3 was previously identified as genetically interacting with Merlin. In this study, the interaction between Merlin and eIF4E 3 was further characterised in the nervous system and male germline of Drosophila as eIF4E 3 expression appears to be restricted to these tissues. Thus, eIF4E 3 may be a candidate for cell type specific modification of Merlin activity. Merlin and eIF4E 3 genetically interact to affect the abundance of neuroblasts in the larval central brain, morphology of the mature testis, and subcellular localisation of eIF4E 3 and Merlin in spermatocytes. Preliminary evidence indicates that Merlin and eIF4E 3 may be able to both increase and decrease translation of transcripts identified as bound to both proteins in vivo, suggesting multiple translational regulatory complexes including Merlin and eIF4E 3 may be formed.

  • Subjects / Keywords
  • Graduation date
    Spring 2016
  • Type of Item
    Thesis
  • Degree
    Master of Science
  • DOI
    https://doi.org/10.7939/R30V8B02M
  • License
    This thesis is made available by the University of Alberta Libraries with permission of the copyright owner solely for non-commercial purposes. This thesis, or any portion thereof, may not otherwise be copied or reproduced without the written consent of the copyright owner, except to the extent permitted by Canadian copyright law.