The VRK1 protein kinase regulates the phosphorylation of BAF, which binds to dsDNA and LEM domain–containing proteins. VRK1 depletion increases the immobile fraction of BAF at the nuclear periphery and disturbs nuclear envelope architecture. It also ...

Phosphorylation of BAF by the vaccinia-related kinase 1 (VRK1) is a key regulator of BAF localization and function. Here, we demonstrate that VRK1 successively phosphorylates BAF on Ser4 and Thr3. The crystal structures of BAF before …

Aug 19, 2020 · Phosphorylation plays a key role in regulating BAF localization and function. The mitotic kinase VRK1/NHK1 phosphorylates BAF in mitosis and meiosis 1, 18 – 20. This phosphorylation weakens the binding of BAF to both chromatin and the LEM-domain proteins 21, and is required for NE disassembly 1, 22.

The pBAF signal at the core region was reduced to 60% by VRK1 siRNA transfection, but was increased by PP4C/R2 siRNA (Fig. 3, A and C). We conclude that the core-localized BAF at early telophase is in the phosphorylated form.

Jan 30, 2023 · Previously reported structures of BAF suggested that it is fully ordered, but our recent NMR analysis revealed that its N-terminal region is flexible in solution and that S4/T3 di-phosphorylation by VRK1 reduces this flexibility.

Jan 15, 2014 · The work presented here confirms a key role for the mammalian VRK1 kinase in regulating the phosphorylation of BAF and its mobility within the NE and also demonstrates that VRK1 depletion leads to mislocalization of BAF during mitosis and …

Mar 21, 2021 · Phosphorylation of BAF by the vaccinia-related kinase 1 (VRK1) is a key regulator of BAF localization and function. Here, we demonstrate that VRK1 successively phosphorylates BAF on Ser4...

Mar 21, 2021 · Phosphorylation of BAF by the vaccinia-related kinase 1 (VRK1) is a key regulator of BAF localization and function. Here, we demonstrate that VRK1 successively phosphorylates BAF on Ser4 and Thr3. The crystal structures of BAF before and after phosphorylation are extremely similar.

The interactions of BAF with its DNA- and protein-binding partners are known to be regulated by phosphorylation, and previously we validated BAF as a highly efficient substrate for the VRK1 protein kinase. Here we show that depletion of VRK1 in MCF10a and MDA-MB-231 cells results in aberrant nuclear architecture.

Recently, it was discovered that early in infection the vaccinia virus (VACV) B12 pseudokinase copurifies with the cellular kinase VRK1, a proviral factor, in the nucleus.