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Publication
The intrinsically disordered region of the cytokinetic F-BAR protein Cdc15
performs a unique essential function in maintenance of cytokinetic ring
integrity.
Authors Mangione MC, Snider CE, Gould KL
Submitted By Submitted Externally on 12/2/2019
Status Published
Journal Molecular biology of the cell
Year 2019
Date Published 10/1/2019
Volume : Pages 30 : 2790 - 2801
PubMed Reference 31509478
Abstract Successful separation of two daughter cells (i.e., cytokinesis) is essential for
life. Many eukaryotic cells divide using a contractile apparatus called the
cytokinetic ring (CR) that associates dynamically with the plasma membrane (PM)
and generates force that contributes to PM ingression between daughter cells. In
Schizosaccharomyces pombe, important membrane-CR scaffolds include the
paralogous F-BAR proteins Cdc15 and Imp2. Their conserved protein structure
consists of the archetypal F-BAR domain linked to an SH3 domain by an
intrinsically disordered region (IDR). Functions have been assigned to the F-BAR
and SH3 domains. In this study we probed the function of the central IDR. We
found that the IDR of Cdc15 is essential for viability and cannot be replaced by
that of Imp2, whereas the F-BAR domain of Cdc15 can be swapped with several
different F-BAR domains, including that of Imp2. Deleting part of the IDR
results in CR defects and abolishes calcineurin phosphatase localization to the
CR. Together these results indicate that Cdc15's IDR has a nonredundant
essential function that coordinates regulation of CR architecture.




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