0000000000037778
AUTHOR
Timo Wagner
Low density lipoprotein receptor-related protein 1 mediated endocytosis of β1-integrin influences cell adhesion and cell migration.
The low density lipoprotein receptor-related protein 1 (LRP1) has been shown to interact with β1-integrin and regulate its surface expression. LRP1 knock-out cells exhibit altered cytoskeleton organization and decreased cell migration. Here we demonstrate coupled endocytosis of LRP1 and β1-integrin and the involvement of the intracellular NPxY2 motif of LRP1 in this process. Mouse embryonic fibroblasts harboring a knock in replacement of the NPxY2 motif of LRP1 by a multiple alanine cassette (AAxA) showed elevated surface expression of β1-integrin and decreased β1-integrin internalization rates. As a consequence, cell spreading was altered and adhesion rates were increased in our cell model…
Partitioning of on-demand electron pairs
The on-demand generation and separation of entangled photon pairs are key components of quantum information processing in quantum optics. In an electronic analogue, the decomposition of electron pairs represents an essential building block for using the quantum state of ballistic electrons in electron quantum optics. The scattering of electrons has been used to probe the particle statistics of stochastic sources in Hanbury Brown and Twiss experiments and the recent advent of on-demand sources further offers the possibility to achieve indistinguishability between multiple sources in Hong-Ou-Mandel experiments. Cooper pairs impinging stochastically at a mesoscopic beamsplitter have been succe…
Stx5 is a novel interactor of VLDL-R to affect its intracellular trafficking and processing
We identified syntaxin 5 (Stx5), a protein involved in intracellular vesicle trafficking, as a novel interaction partner of the very low density lipoprotein (VLDL)-receptor (VLDL-R), a member of the LDL-receptor family. In addition, we investigated the effect of Stx5 on VLDL-R maturation, trafficking and processing. Here, we demonstrated mutual association of both proteins using several in vitro approaches. Furthermore, we detected a special maturation phenotype of VLDL-R resulting from Stx5 overexpression. We found that Stx5 prevented advanced Golgi-maturation of VLDL-R, but did not cause accumulation of the immature protein in ER, ER to Golgi compartments, or cis-Golgi ribbon, the main ex…