2 edition of Identification of novel neurofibromin interacting proteins using epitope-tagged domains and mass spectrometry. found in the catalog.
Identification of novel neurofibromin interacting proteins using epitope-tagged domains and mass spectrometry.
Neurofibromatosis Type 1 (NF1) is a common tumor predisposition syndrome in humans. The NF1 gene encodes the Ras-GAP neurofibromin. Loss of neurofibromin results in elevated levels of Ras signaling, underlying neoplastic manifestations of NF1 but not readily explaining its many non-neoplastic features. This leads to the hypothesis of this thesis: there exist additional normal neurofibromin-protein interaction(s) and therefore function(s) outside of its GAP domain, the loss of which may contribute to the NF1 phenotype.Employing a GST epitope-tagged Tubulin Binding Domain (GST-TBD) bait, alpha-tubulin, dynein, and Leucine Rich Pentatrico Peptide Repeat Cassette protein (LRPPRC) were identified from human Schwann cell lysates. Verification of the neurofibromin-LRPPRC interaction was undertaken by multiple molecular techniques. The results herein suggest that LRPPRC is a valid in vivo interactor with the neurofibromin-TBD. Confirmatory data requires a more specific neurofibromin antibody. These results are consistent with an emerging model of neurofibromin activity in intracellular vesicle transport.
|The Physical Object|
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