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Ninein domains required for its localization, association with partners dynein and ensconsin, and microtubule organization

Ninein domains required for its localization, association with partners dynein and ensconsin, and microtubule organization

FromPaperPlayer biorxiv cell biology


Ninein domains required for its localization, association with partners dynein and ensconsin, and microtubule organization

FromPaperPlayer biorxiv cell biology

ratings:
Length:
20 minutes
Released:
Jun 22, 2023
Format:
Podcast episode

Description

Link to bioRxiv paper:
http://biorxiv.org/cgi/content/short/2023.06.22.546109v1?rss=1

Authors: Tillery, M. M. L., Zheng, C., Zheng, Y., Megraw, T. L.

Abstract:
Ninein (Nin) is a microtubule (MT) anchor at the subdistal appendages of mother centrioles and the pericentriolar material (PCM) of centrosomes that also functions to organize microtubules at non-centrosomal microtubule-organizing centers (ncMTOCs). In humans, the NIN gene is mutated in Seckel syndrome, an inherited developmental disorder. Here we dissect the protein domains involved in Nin's localization and interactions with dynein and ensconsin (ens/MAP7) and show that the association with ens cooperatively regulates microtubule assembly in Drosophila fat body cells. We define domains of Nin responsible for its localization to the ncMTOC on the fat body cell nuclear surface, localization within the nucleus, and association with Dynein light intermediate chain (Dlic) and ens, respectively. We show that Nin's association with ens synergistically regulates MT assembly. Together, these findings reveal novel features of Nin function and its regulation of a ncMTOC.

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Podcast created by Paper Player, LLC
Released:
Jun 22, 2023
Format:
Podcast episode

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