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Start Over Author "Sandra Krull" Topic nuclear pore complex
2 results on '"Sandra Krull"'

1. ZC3HC1 Is a Novel Inherent Component of the Nuclear Basket, Resident in a State of Reciprocal Dependence with TPR

Author

Philip Gunkel, Haruki Iino, Sandra Krull, and Volker C. Cordes

Subjects
NIPA, nuclear basket, nuclear interacting partner of ALK, nuclear pore complex, nucleoprotein TPR, translocated promoter region, Cytology, QH573-671
Abstract

The nuclear basket (NB) scaffold, a fibrillar structure anchored to the nuclear pore complex (NPC), is regarded as constructed of polypeptides of the coiled-coil dominated protein TPR to which other proteins can bind without contributing to the NB’s structural integrity. Here we report vertebrate protein ZC3HC1 as a novel inherent constituent of the NB, common at the nuclear envelopes (NE) of proliferating and non-dividing, terminally differentiated cells of different morphogenetic origin. Formerly described as a protein of other functions, we instead present the NB component ZC3HC1 as a protein required for enabling distinct amounts of TPR to occur NB-appended, with such ZC3HC1-dependency applying to about half the total amount of TPR at the NEs of different somatic cell types. Furthermore, pointing to an NB structure more complex than previously anticipated, we discuss how ZC3HC1 and the ZC3HC1-dependent TPR polypeptides could enlarge the NB’s functional repertoire.

Published
2021
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2. Protein Tpr is required for establishing nuclear pore-associated zones of heterochromatin exclusion

Author

Sandra Krull, Sonja Reidenbach, Julia Dörries, Helene Norder, Johan Thyberg, Bjorn M. M. Boysen, Volker C. Cordes, and Lars O. Magnius

Subjects
Euchromatin, Somatic cell, Heterochromatin, Tpr, Biology, Models, Biological, Article, General Biochemistry, Genetics and Molecular Biology, Mice, Prophase, Microscopy, Electron, Transmission, RNA interference, nuclear pore complex, Proto-Oncogene Proteins, medicine, Animals, Humans, Gene Silencing, Nuclear pore, Molecular Biology, Cell Nucleus, Microscopy, Confocal, General Immunology and Microbiology, nuclear compartmentalization, General Neuroscience, heterochromatin, Molecular biology, Chromatin, Cell biology, Nuclear Pore Complex Proteins, Poliovirus, Cell nucleus, medicine.anatomical_structure, Microscopy, Fluorescence, RNA Interference, HeLa Cells
Abstract

Amassments of heterochromatin in somatic cells occur in close contact with the nuclear envelope (NE) but are gapped by channel- and cone-like zones that appear largely free of heterochromatin and associated with the nuclear pore complexes (NPCs). To identify proteins involved in forming such heterochromatin exclusion zones (HEZs), we used a cell culture model in which chromatin condensation induced by poliovirus (PV) infection revealed HEZs resembling those in normal tissue cells. HEZ occurrence depended on the NPC-associated protein Tpr and its large coiled coil-forming domain. RNAi-mediated loss of Tpr allowed condensing chromatin to occur all along the NE's nuclear surface, resulting in HEZs no longer being established and NPCs covered by heterochromatin. These results assign a central function to Tpr as a determinant of perinuclear organization, with a direct role in forming a morphologically distinct nuclear sub-compartment and delimiting heterochromatin distribution.

Published
2010
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