Philip Gunkel

@philipgunkel.bsky.social
Postdoc @mpi_nat; Research focus: the nuclear pore complex and in particular the nuclear basket - composition and function.

[Philip Gunkel @GunkelPhilip]

See you on the other (hopefully brighter) side: @philipgunkel.bsky.social

[Philip Gunkel @GunkelPhilip]

@lab_engel Congratulations Christoph! Well deserved.

[Philip Gunkel @GunkelPhilip]

@NicholasAder Congratulations Nick!

[The EMBO Journal @embojournal]

A nanobody toolkit for tracking or blocking nuclear pore complex (NPC) biogenesis identifies a checkpoint linking assembly of the NPC scaffold to formation of the Np98-dominated permeability barrier

Dirk Görlich and coworkers
@NPC_aficionado @mpi_nat

https://t.co/Ff0EU5MMBJ

[Philip Gunkel @GunkelPhilip]

@ribonucleicacid Congratulation Alex!

[Philip Gunkel @GunkelPhilip]

@AndImaging @aaandmoore ....and heterochromatin exclusion zones (HEZs) are formed by so-called nuclear baskets, which keep the nuclear pores free (https://t.co/rnCpCW8jgz)

[Philip Gunkel @GunkelPhilip]

How I sort GFP-tagged cells ...

[Science girl @sciencegirl]

Optical sorting technology that separates green and red tomatoes

[Karsten Weis Lab @KarstenWeisLab]

Congratulations to Janka Zsok and Elisa Dultz for their paper on the #nuclearpore basket in collaboration with @LucienWeissLab. The first preprint from the Dultz group!
"doRITE" and have a look at tracks of single NPCs.
https://t.co/U14i91BZRX

[Philip Gunkel @GunkelPhilip]

@Schliekerlab Congratulations, Christian. Well deserved!

[Institut Jacques Monod @IJMonod]

✍️The Doye Lab's (@DoyeValerie) new article "Y-complex nucleoporins independently contribute to nuclear pore assembly and gene regulation in neuronal progenitors" made the cover and the highlight of @J_Cell_Sci 👏
➡️https://t.co/f88bSJpqwH
⬇️https://t.co/3mk5Ppqckp

[Philip Gunkel @GunkelPhilip]

9/9 Finally, the ZC3HC1 structure predictions by AlphaFold2 illustrate an evolutionarily conserved NuBaID construction and enabled the redefinition of BLD boundaries. These predictions are consistent with the recent crystal structure of Pml39p by Hashimoto et al. @PalancadeLab.

[Philip Gunkel @GunkelPhilip]

8/9 We have further demonstrated that Pml39p enables interlinkage of Mlp1 polypeptides in nuclear foci in the absence of Nup60p. These results for the budding yeast protein Pml39 are consistent with features that we previously described for human ZC3HC1 (https://t.co/F0BE8PjjvZ).

[Philip Gunkel @GunkelPhilip]

7/9 It was already known that Pml39p is a Mlp-interacting protein (Palancade et al. 2005 @DoyeValerie). We have now shown that Pml39p is required for positioning Mlp1p subpopulations at the NB, in line with a recent report by Bensidoun et al. @BensPierre4 @rnp_biology @zenklusd

[Philip Gunkel @GunkelPhilip]

6/9 We found DdZC3HC1 colocalizing with DdTPR at the nuclear envelope of D. discoideum Ax2 cells with an offset toward the nuclear interior relative to the labelling of FG-nucleoporins.

[Philip Gunkel @GunkelPhilip]

5/9 We further investigated the identified ZC3HC1 homologues of Dictyostelium discoideum (DdZC3HC1) and Saccharomyces cerevisiae (ScPml39p; already mentioned in Gunkel et al, 2021), which share the same characteristic and unique bimodular NuBaID signature.

[Philip Gunkel @GunkelPhilip]

4/9 We show that such a bimodular construction is evolutionarily conserved and allows the identification of a ZC3HC1 homologue in most taxa of the eukaryotic realm. Interestingly, no homologue can be identified in the famous model organism Drosophila.

[Philip Gunkel @GunkelPhilip]

1/9 Finally, in press @MBoCjournal: our description of the evolutionary conserved TPR-/Mlp-binding domain of ZC3HC1/Pml39p. https://t.co/Bzga79484i

[Philip Gunkel @GunkelPhilip]

3/9 Both domains (called BLD1 and BLD2) are required to establish a functional TPR-binding interface. These two BLDs are zinc finger domains that form an experimentally validated functional unit, which we have named NuBaID (nuclear basket interaction domain).

[Philip Gunkel @GunkelPhilip]

2/9 We describe the molecular prop­erties of ZC3HC1 that enable its initial binding to the nuclear basket (NB) and TPR. First, we mapped the minimal bimodular interaction domain of human ZC3HC1. Any further truncations resulted in loss of NB binding of such ZC3HC1 mutants.

[Philip Gunkel @GunkelPhilip]

@J_Bucevicius @NatureComms Great work. Congrats Jonas & colleagues