Please use this identifier to cite or link to this item: http://dx.doi.org/10.25673/119358
Title: Lipid-binding features and phosphoinositide-dependent function of the endocytic adaptor protein 2 (AP2)-complex from Arabidopsis thaliana
Author(s): Uhlenberg, JohannaLook up in the Integrated Authority File of the German National Library
Referee(s): Heilmann, IngoLook up in the Integrated Authority File of the German National Library
Peiter, EdgarLook up in the Integrated Authority File of the German National Library
Isono, ErikaLook up in the Integrated Authority File of the German National Library
Granting Institution: Martin-Luther-Universität Halle-Wittenberg
Issue Date: 2025
Extent: 1 Online-Ressource (XI, 134 Seiten)
Type: HochschulschriftLook up in the Integrated Authority File of the German National Library
Type: PhDThesis
Exam Date: 2025-06-26
Language: English
URN: urn:nbn:de:gbv:3:4-1981185920-1213164
Abstract: Regulation of plasma membrane (PM) composition is crucial for plant cell function. Clathrin-mediated endocytosis (CME) is a key pathway for protein internalization from the PM. This study explores how anionic phospholipids, particularly phosphoinositides (PIs) regulate CME in Arabidopsis. Mutants with disrupted PI metabolism showed altered membrane order and impaired endocytosis. The AP2-complex, crucial for CME initiation, was found to directly bind PIs, especially PtdIns(4,5)P2, via polybasic regions. Mutated AP2-subunits with reduced lipid binding led to defective CME, as shown by reduced FM4-64 uptake and altered cargo internalization. AP2-subunits interacted with various lipid kinases important for PI biosynthesis, including PIP5K1, PIP5K2 and PIP5K6, which have been functionally implicated in CME. These findings suggest that PtdIns(4,5)P2 modulates CME through direct interaction with AP2, highlighting a molecular mechanism linking PI-metabolism to membrane trafficking in plants.
Annotations: Seiten gezählt als 1-95, XCVI-CXXXIV
URI: https://opendata.uni-halle.de//handle/1981185920/121316
http://dx.doi.org/10.25673/119358
Open Access: Open access publication
License: (CC BY 4.0) Creative Commons Attribution 4.0(CC BY 4.0) Creative Commons Attribution 4.0
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