An inducible two-component CRISPR-based platform that rapidly repositions HSV-1 genomes to the nuclear edge unveils intranuclear space heterogeneity for the incoming viral genomes and dynamic stages of the host-virus interplay during early infection.
Nana Naetar, Konstantina Georgiou ... Roland Foisner
The lamin A/C binding protein LAP2α inhibits formation of higher order lamin structures in the nuclear interior in a lamin A/C-phosphorylation-independent manner, thereby regulating chromatin mobility.
Calcium release from the endoplasmic reticulum through the IP3 receptor ion channel is strongly regulated by a calcium-binding protein in the lumen of the endoplasmic reticulum.
The INM protein LAP1B, an activator of Torsin ATPases, is a chromatin-binding factor that erroneously persists on mitotic chromatin if Torsin functionality is compromised, inducing chromosome segregation defects and binucleation.
A systemic proteome of the pellicle organelle inner membrane complex (IMC) provides new insight for the intraerythrocytic proliferation of malaria parasite and identifies the palmitoyl-acyl-transferase DHHC2 as a key enzyme regulating the localization of IMC proteins through palmitoylation.
Efficient targeting of membrane proteins from the endoplasmic reticulum (ER) to the inner nuclear membrane depends on GTP hydrolysis by Atlastin GTPases and their function in maintaining an interconnected topology of the ER network.
The super-resolution fluorescence microscopy approach polarization PALM (p-PALM) reveals that macromolecular crowding and inhomogeneity within nuclear pores generate a structurally and dynamically complex permeability barrier.
