Multicolor single molecule localization microscopy to monitor the organization of the golgi complex
Visualitza/Obre
MasterThesis_CarmenARodilla.pdf (2,455Mb) (Accés restringit)
appendix_MasterThesis_CarmenARodilla.zip (116,6Kb) (Accés restringit)
Estadístiques de LA Referencia / Recolecta
Inclou dades d'ús des de 2022
Cita com:
hdl:2117/343345
Tipus de documentProjecte Final de Màster Oficial
Data2020-11-26
Condicions d'accésAccés restringit per decisió de l'autor
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Abstract
The Golgi complex is the central organelle of the secretory pathway, where it plays akey role in protein sorting, transport and processing. Despite its huge importance, light-microscopy-based studies of the Golgi complex have been limited by its very dynamic char-acter and small size. In this project, we used super-resolution microscopy tools to understandthe functional compartmentalization of the Golgi membranes at the nanoscale. In particular,we were interested in understanding how the processing, sorting, and export of proteins areorganized in space and time at the trans-Golgi network (TGN), the final sorting station ofthis organelle. We specifically studied the influence of the transmembrane domain of a cargoprotein, TGN46, and a resident enzyme, sialyltransferase (ST), in the lateral localizationof these proteins along the TGN. We co-expressed different mutants of these proteins inhuman cells, processed them for imaging by two different super-resolution nanoscopy tech-inques (STED and STORM), and quantitatively measured their degree of colocalization.Our results highlight the fact that the length and amino acid composition of these proteinsdoes not seem to be a main driver for their precise intra-Golgi localization.
Col·leccions
Fitxers | Descripció | Mida | Format | Visualitza |
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MasterThesis_CarmenARodilla.pdf | 2,455Mb | Accés restringit | ||
appendix_MasterThesis_CarmenARodilla.zip | 116,6Kb | application/zip | Accés restringit |