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Griffin, J. N.

Publications and source records attributed to Griffin, J. N..

2 recordsLinked to original sources

WDR5 stabilizes actin architecture to promote multiciliated cell formation

HIGHLIGHTS O_LIWDR5 has an H3K4 independent role in the formation of multiciliated cells.\nC_LIO_LIWDR5 controls apical cell expansion, basal body patterning, and ciliogenesis in multiciliated cells.\nC_LIO_LIWDR5 localizes near the ciliary base where it connects basal bodies to F-actin.\nC_LIO_LIWDR5 stabilizes the apical actin network in multiciliated cells.\nC_LI\n\nSUMMARYThe actin cytoskeleton is critical to shape cells and pattern intracellular organelles to drive tissue morphogenesis. In multiciliated cells (MCCs), apical actin forms a lattice that drives expansion of the cell surface necessary to host hundreds of cilia. The actin lattice also uniformly distributes basal bodies across this surface. This apical actin network is dynamically remodeled, but the molecules that regulate its architecture remain poorly understood. We identify the chromatin modifier, WDR5, as a regulator of apical F-actin in multiciliated cells. Unexpectedly, WDR5 functions independently of chromatin modification in MCCs. Instead, we discover a scaffolding role for WDR5 between the basal body and F-actin. Specifically, WDR5 binds to basal bodies and migrates apically, where F-actin organizes around WDR5. Using a monomer trap for G-actin, we show that WDR5 stabilizes F-actin to maintain apical lattice architecture. In summary, we identify a novel, non-chromatin role for WDR5 in stabilizing F-actin in multiciliated cells.\n\nIN BRIEFKulkarni et al discover a chromatin independent function for WDR5 in multiciliated cell formation. WDR5 localizes to the base of cilia and functions as a scaffold between the basal bodies and the apical actin lattice. There, WDR5 stabilizes the actin lattice that allows multiciliated cells to expand their apical surface, pattern basal bodies, and generate hundreds of cilia.

developmental biology

RAPGEF5 regulates nuclear transport of β-catenin

Canonical Wnt signaling coordinates many critical aspects of embryonic development, while dysregulated Wnt signaling contributes to common diseases, including congenital malformations and cancer. The nuclear localization of {beta}-catenin is the defining step in pathway activation. However, despite intensive investigation, the mechanisms regulating {beta}-catenin nuclear transport remain undefined. In a patient with congenital heart disease and heterotaxy, a disorder of left-right patterning, we previously identified the guanine nucleotide exchange factor, RAPGEF5. Here, we demonstrate that RAPGEF5 regulates left-right patterning via Wnt signaling. In particular, RAPGEF5, regulates the nuclear translocation of {beta}-catenin independently of both {beta}-catenin cytoplasmic stabilization and the importin {beta}1/Ran mediated transport system. We propose a model whereby RAPGEF5 activates the nuclear GTPases, Rap1/2, to facilitate the nuclear transport of {beta}-catenin, defining a parallel nuclear transport pathway to Ran. Our results suggest new targets for modulating Wnt signaling in disease states.

developmental biology