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Identification and characterization of a novel interaction between cask and the transforming growth factor beta receptor interacting protein

Membrane-associated guanylate kinases (MAGUKs) are a family of molecular scaffolds that organize and cluster protein complexes at subcellular specializations. CASK, a multimodular MAGUK containing CamK, PDZ, SH3 and GK domains, is involved in a variety of molecular events including EGF receptor localization and signalling, KIF-17 dependent NMDA receptor containing vesicle transport, presynaptic vesicle exocytosis and basolateral localization of certain transmembrane proteins. CASK also translocates to the nucleus upon interaction with the Tbr-1 transcription factor where it functions as a transcription regulator. We used the CASK PDZ domain in a yeast two-hybrid screen to identify novel members involved in CASK function. TRIP, a TGF-beta Receptor II (TBRII) Interacting Protein that modulates TBRII-dependent gene expression, was identified as a CASK binding protein through its consensus C-terminal PDZ type-II interacting motif. Here we show that CASK, TRIP and TBRII interact in vitro assays, heterologous expression systems and form a tripartite complex in brain.

Identiferoai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.78377
Date January 2002
CreatorsHo, Joanne Wing Yee, 1977-
ContributorsShrier, Alvin (advisor)
PublisherMcGill University
Source SetsLibrary and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada
LanguageEnglish
Detected LanguageEnglish
TypeElectronic Thesis or Dissertation
Formatapplication/pdf
CoverageMaster of Science (Department of Physiology.)
RightsAll items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated.
Relationalephsysno: 001974447, proquestno: AAIMQ88212, Theses scanned by UMI/ProQuest.

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