Nuclear pore complex: structure and function

info:eu-repo/semantics/publishe

Nup153, a keeper of genome integrity?

info:eu-repo/semantics/nonPublishe

Rank-ligand bypasses lymphoid tissue-inducing cells in post-natal lymph node

info:eu-repo/semantics/nonPublishe

Modulation of epidermo-pilosebaceous unit epithelial cell proliferation via RANK.

info:eu-repo/semantics/publishe

Structural characterization of altered nucleoporin Nup153 expression in human cells by thin-section electron microscopy.

Nuclear pore complexes (NPCs) span the 2 membranes of the nuclear envelope (NE) and facilitate nucleocytoplasmic exchange of macromolecules. NPCs have a roughly tripartite structural organization with the so-called nuclear basket emanating from the NPC scaffold into the nucleoplasm. The nuclear basket is composed of the 3 nucleoporins Nup153, Nup50, and Tpr, but their specific role for the structural organization of this NPC substructure is, however, not well established. In this study, we have used thin-section transmission electron microscopy to determine the structural consequences of altering the expression of Nup153 in human cells. We show that the assembly and integrity of the nuclear basket is not affected by Nup153 depletion, whereas its integrity is perturbed in cells expressing high concentrations of the zinc-finger domain of Nup153. Moreover, even mild over-expression of Nup153 is coinciding with massive changes in nuclear organization and it is the excess of the zinc-finger domain of Nup153 that is sufficient to induce these rearrangements. Our data indicate a central function of Nup153 in the organization of the nucleus, not only at the periphery, but throughout the entire nuclear interior.SCOPUS: ar.jinfo:eu-repo/semantics/publishe

Regeneration of hair and epidermis by the receptor activator of NF-kappaB

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Localisation of Nup153 and SENP1 to nuclear pore complexes is required for 53BP1 mediated DNA double-strand break repair.

The nuclear basket of nuclear pore complexes (NPCs) is composed of three nucleoporins: Nup153, Nup50 and Tpr. Nup153 has a role in DNA double-strand break (DSB) repair by promoting nuclear import of 53BP1, a mediator of DNA damage response. Here we provide evidence that loss of Nup153 compromises 53BP1 sumoylation, prerequisite for efficient accumulation of 53BP1 at DSBs. Depletion of Nup153 resulted in reduced SUMO1 modification of 53BP1 and the displacement of the SUMO protease SENP1 from NPCs. Artificial tethering of SENP1 to NPCs restored non-homologous end joining (NHEJ) in the absence of Nup153 and re-established 53BP1 sumoylation. Furthermore, Nup50 and Tpr, the two other nuclear basket nucleoporins, also contribute to proper DSB repair, in a manner distinct from Nup153. Similar to Nup153, Tpr appears implicated in NHEJ and homologous recombination (HR), whereas loss of Nup50 only affected NHEJ. Despite the requirement of all three nucleoporins for accurate NHEJ, only Nup153 is needed for proper nuclear import of 53BP1and SENP1-dependent sumoylation of 53BP1. Our data support the role of Nup153 as important regulator of 53BP1 activity and efficient NHEJ.SCOPUS: ar.jinfo:eu-repo/semantics/publishe

Hair follicle RANK-ligand regulates epithelial growth via Bcl-3

info:eu-repo/semantics/nonPublishe

Bimodal labeling of lipopolysaccharides (LPS) for SPECT-CT and fluorescence dual imaging

info:eu-repo/semantics/nonPublishe

Bimodal labeling of lipopolysaccharides (LPS) for SPECT-CT and fluorescence dual imaging

info:eu-repo/semantics/nonPublishe