Publications by authors named "Lene E Olesen"
Adaptor protein (AP) complexes bind to transmembrane proteins destined for internalization and to membrane lipids, so linking cargo to the accessory internalization machinery. This machinery interacts with the appendage domains of APs, which have platform and beta-sandwich subdomains, forming the binding surfaces for interacting proteins. Proteins that interact with the subdomains do so via short motifs, usually found in regions of low structural complexity of the interacting proteins.
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- Clathrin-mediated endocytosis involves a network of proteins that helps select cargo and shape the membrane to form vesicles.
- The adaptor protein (AP) appendage domains serve as crucial protein interaction hubs, binding to specific peptide motifs from synaptojanin.
- The interactions of these appendages with their binding partners are essential for the clustering and functionality needed in the vesicle assembly process, emphasizing that the status of these interactions is temporary and critical for proper vesicle formation.
EpsinR is a clathrin-coated vesicle (CCV) enriched 70-kD protein that binds to phosphatidylinositol-4-phosphate, clathrin, and the gamma appendage domain of the adaptor protein complex 1 (AP1). In cells, its distribution overlaps with the perinuclear pool of clathrin and AP1 adaptors. Overexpression disrupts the CCV-dependent trafficking of cathepsin D from the trans-Golgi network to lysosomes and the incorporation of mannose-6-phosphate receptors into CCVs.
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