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Sunday, August 2, 2020 | History

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.

Joseph Wiley

Identification of novel neurofibromin interacting proteins using epitope-tagged domains and mass spectrometry.

by Joseph Wiley

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About the Edition

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
Pagination124 leaves.
Number of Pages124
ID Numbers
Open LibraryOL21218915M
ISBN 109780494273760


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