Cyclin-dependent kinase 1 depolymerizes nuclear lamin filaments by disrupting the head-to-tail interaction of the lamin central rod domain

Lamin Filament Assembly Derived from the Atomic Structure of the Antiparallel Four-Helix Bundle

“…The parallel four-helix bundle models were built to represent the ACN binding mode of coil 2C and coil 1a suggested by Makarov et al (2019) and Stalmans et al (2020) . We built this model by trimming and refining the four-helix bundle models used in the previous research ( Jeong et al, 2022 ). Then, this model (residues 338-381 in the coil 2C part) was linked to the C-terminal ends of the A22 four-helix bundle model (residues 244-337) ( Figs.…”

Chemically induced proximity reveals mechanotransduction of a meiotic checkpoint at the nuclear envelope

“…In mice, the kinase Cdk2 localizes to both telomeres and CO sites, and is essential to link telomeres to the NE to form the "meiotic bouquet" (90; 91). Vertebrate CDKs phosphorylate lamins to disassemble the NE in mitosis (92)(93)(94)(95) and Cdk2 may thus also modulate NE dynamics during meiotic prophase. DSB formation, which is essential for CO formation, is important for timely bouquet resolution (96).…”

Are the Head and Tail Domains of Intermediate Filaments Really Unstructured Regions?

“…In fact, posttranslational modifications (PTMs), such as phosphorylation events, control the assembly stage of IFs and thus control the interactions between different proteins affecting IF function in processes such as cell migration, cell mitosis, and stress responses [72]. Furthermore, the head domain acts as a recipient of multiple post-translational modifications regulating the dynamic assembly-disassembly process of the IF network and contributes to maintaining the structural and functional integrity of IFs [72][73][74][75]. Important interactions between IFs and other cellular components and structures are catalyzed through PTMs [76].…”