Tesi etd-06062019-151511 |
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Tipo di tesi
Tesi di laurea magistrale
Autore
CECCARELLI, LORENZO
URN
etd-06062019-151511
Titolo
Subcellular localization and interactions of nerve growth factor receptors TrkA and p75NTR
Dipartimento
BIOLOGIA
Corso di studi
BIOTECNOLOGIE MOLECOLARI
Relatori
relatore Dott.ssa Marchetti, Laura
relatore Prof. Cecchini, Marco
correlatore Prof.ssa Raffa, Vittoria
correlatore Prof. Cammalleri, Maurizio
relatore Prof. Cecchini, Marco
correlatore Prof.ssa Raffa, Vittoria
correlatore Prof. Cammalleri, Maurizio
Parole chiave
- extracellular vesicles
- interactomics
- Neurotrophins receptor
- p75NTR
- single particle tracking
- TrkA
Data inizio appello
15/07/2019
Consultabilità
Non consultabile
Data di rilascio
15/07/2089
Riassunto
My master thesis work is part of a research project concerning the study of subcellular localization and dynamics of neurotrophin membrane receptors. To this purpose, my group has developed in the last years a method for site-directed and stoichiometry-controlled enzymatic labeling of neurotrophins and their receptors working in vitro on purified neurotrophins, as well as on living cells where it achieves selective labeling of surface-exposed neurotrophin receptors.
During my thesis work, I managed to produce and purify an enzyme for neurotrophin receptor labeling and used this tool to characterize the time-dependent variation of cell surface density of WT, K544N and R649W TrkA receptors in response to NGF. In parallel, TAP-tagged constructs of TrkA variants will allow the recovery of protein extracts highly enriched in TrkA and relative interactors to be analyzed by mass spectrometry. Finally, I produced extracellular vesicles containing p75NTR, which are currently being analyzed by our collaborators.
During my thesis work, I managed to produce and purify an enzyme for neurotrophin receptor labeling and used this tool to characterize the time-dependent variation of cell surface density of WT, K544N and R649W TrkA receptors in response to NGF. In parallel, TAP-tagged constructs of TrkA variants will allow the recovery of protein extracts highly enriched in TrkA and relative interactors to be analyzed by mass spectrometry. Finally, I produced extracellular vesicles containing p75NTR, which are currently being analyzed by our collaborators.
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