Evidence for an interaction of paracingulin with microtubules

The mechanisms that anchor microtubules to epithelial junctions are poorly understood. Here we show that recombinant purified paracingulin ( CGNL1 , JACOP), a cytoplasmic junctional protein, decorates microtubules by negative staining electron microscopy and co-pellets with microtubules. Co-pelletin...

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Bibliographic Details
Published inmicroPublication biology Vol. 2024
Main Authors Flinois, Arielle, Mutero-Maeda, Annick, Montessuit, Sylvie, Citi, Sandra
Format Journal Article
LanguageEnglish
Published United States Caltech Library 2024
Subjects
Biochemistry
Human
New Finding
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Summary:The mechanisms that anchor microtubules to epithelial junctions are poorly understood. Here we show that recombinant purified paracingulin ( CGNL1 , JACOP), a cytoplasmic junctional protein, decorates microtubules by negative staining electron microscopy and co-pellets with microtubules. Co-pelleting experiments using fragments of CGNL1 indicate that this is mediated by a central region of the CGNL1 head domain (residues 250-420). Deletion of a basic amino-acid stretch (365-377) within this fragment, abolishes both co-pelleting with and decoration of microtubules. These results suggest that paracingulin can interact directly with microtubules through a basic amino-acid stretch of its head domain.
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The authors declare that there are no conflicts of interest present.
ISSN:2578-9430
2578-9430
DOI:10.17912/micropub.biology.001341