PT  - JOURNAL ARTICLE
AU  - Sarah Mermet
AU  - Maxime Voisin
AU  - Joris Mordier
AU  - Tristan Dubos
AU  - Sylvie Tutois
AU  - Pierre Tuffery
AU  - Célia Baroux
AU  - Kentaro Tamura
AU  - Aline V. Probst
AU  - Emmanuel Vanrobays
AU  - Christophe Tatout
TI  - Evolutionary conserved protein motifs drive attachment of the plant nucleoskeleton at nuclear pores
AID  - 10.1101/2021.03.20.435662
DP  - 2021 Jan 01
TA  - bioRxiv
PG  - 2021.03.20.435662
4099  - http://biorxiv.org/content/early/2021/03/20/2021.03.20.435662.short
4100  - http://biorxiv.org/content/early/2021/03/20/2021.03.20.435662.full
AB  - The nucleoskeleton forms a filamentous meshwork under the nuclear envelope and contributes to the regulation of nuclear morphology and gene expression. To understand how the Arabidopsis nucleoskeleton physically connects to the nuclear periphery, we investigated the nucleoskeleton protein KAKU4 and sought for functional regions responsible for its localization at the nuclear periphery. Computational predictions identified three evolutionary conserved peptide motifs within the N-terminal region of KAKU4. Functional analysis revealed that these motifs are required for homomerization of KAKU4, interaction with the nucleoskeleton proteins CROWDED NUCLEI (CRWN) and localization at the nuclear periphery. We find that similar protein motifs are present in NUP82 and NUP136, two plant specific nucleoporins from the Nuclear Pore Complex (NPC) basket. These conserved motifs allow the two nucleoporins to bind CRWN proteins, thus revealing a physical link between the nucleoskeleton and nuclear pores in plants. Finally, whilst NUP82, NUP136 and KAKU4 have a common evolutionary history predating non-vascular land plants, KAKU4 mainly localizes outside the NPC suggesting neofunctionalization of an ancient nucleoporin into a new nucleoskeleton component.Competing Interest StatementThe authors have declared no competing interest.