Format:
1 Online-Ressource (106 Seiten, 9548 KB)
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Illustrationen, Diagramme
Content:
In plant cells, subcellular transport of cargo proteins relies to a large extent on post-Golgi transport pathways, many of which are mediated by clathrin-coated vesicles (CCVs). Vesicle formation is facilitated by different factors like accessory proteins and adaptor protein complexes (APs), the latter serving as a bridge between cargo proteins and the coat protein clathrin. One type of accessory proteins is defined by a conserved EPSIN N-TERMINAL HOMOLOGY (ENTH) domain and interacts with APs and clathrin via motifs in the C-terminal part. In Arabidopsis thaliana, there are three closely related ENTH domain proteins (EPSIN1, 2 and 3) and one highly conserved but phylogenetically distant outlier, termed MODIFIED TRANSPORT TO THE VACUOLE1 (MTV1). In case of the trans-Golgi network (TGN) located MTV1, clathrin association and a role in vacuolar transport have been shown previously (Sauer et al. 2013). In contrast, for EPSIN1 and EPSIN2 limited functional and localization data were available; and EPSIN3 remained completely uncharacterized ...
Note:
Dissertation Universität Potsdam 2022
Additional Edition:
Erscheint auch als Druck-Ausgabe Tegtmeier, Laura Functional analysis of ENTH domain proteins Potsdam, 2022
Language:
English
Keywords:
Hochschulschrift
DOI:
10.25932/publishup-57004
URN:
urn:nbn:de:kobv:517-opus4-570049
Author information:
Großmann, Guido 1978-