Format:
1 Online-Ressource (XIII, 156 Seiten, 31300 KB)
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Content:
This work analyzed functional and regulatory aspects of the so far little characterized EPSIN N-terminal Homology (ENTH) domain-containing protein EPSINOID2 in Arabidopsis thaliana. ENTH domain proteins play accessory roles in the formation of clathrin-coated vesicles (CCVs) (Zouhar and Sauer 2014). Their ENTH domain interacts with membranes and their typically long, unstructured C-terminus contains binding motifs for adaptor protein complexes and clathrin itself. There are seven ENTH domain proteins in Arabidopsis. Four of them possess the canonical long C-terminus and participate in various, presumably CCV-related intracellular transport processes (Song et al. 2006; Lee et al. 2007; Sauer et al. 2013; Collins et al. 2020; Heinze et al. 2020; Mason et al. 2023). The remaining three ENTH domain proteins, however, have severely truncated C-termini and were termed EPSINOIDs (Zouhar and Sauer 2014; Freimuth 2015). Their functions are currently unclear. Preceding studies focusing on EPSINOID2 indicated a role in root hair formation: epsinoid2 T DNA mutants exhibited an increased root hair density and EPSINOID2-GFP was specifically located in non-hair cell files in the Arabidopsis root epidermis (Freimuth 2015, 2019). [...]
Note:
Dissertation Universität Potsdam 2024
Additional Edition:
Erscheint auch als Druck-Ausgabe Freimuth, Nina Elucidating the suppression of root hair formation by a member of a novel, short ENTH protein family in Arabidopsis thaliana Potsdam, 2024
Language:
English
Keywords:
Hochschulschrift
DOI:
10.25932/publishup-63499
URN:
urn:nbn:de:kobv:517-opus4-634994