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Filamin A- and formin 2-dependent endocytosis regulates proliferation via the canonical Wnt pathway

G. Lian, M. Dettenhofer, J. Lu, M. Downing, A. Chenn, T. Wong, V. Sheen,

. 2016 ; 143 (23) : 4509-4520. [pub] 20161027

Jazyk angličtina Země Anglie, Velká Británie

Typ dokumentu časopisecké články

Perzistentní odkaz   https://www.medvik.cz/link/bmc17031324
E-zdroje Online Plný text

NLK Free Medical Journals od 1953 do Před 6 měsíci
Open Access Digital Library od 1953-03-01 do Před 6 měsíci

Odkazy

PubMed 27789627
DOI 10.1242/dev.139295
Knihovny.cz E-zdroje

Actin-associated proteins regulate multiple cellular processes, including proliferation and differentiation, but the molecular mechanisms underlying these processes are unclear. Here, we report that the actin-binding protein filamin A (FlnA) physically interacts with the actin-nucleating protein formin 2 (Fmn2). Loss of FlnA and Fmn2 impairs proliferation, thereby generating multiple embryonic phenotypes, including microcephaly. FlnA interacts with the Wnt co-receptor Lrp6. Loss of FlnA and Fmn2 impairs Lrp6 endocytosis, downstream Gsk3β activity, and β-catenin accumulation in the nucleus. The proliferative defect in Flna and Fmn2 null neural progenitors is rescued by inhibiting Gsk3β activity. Our findings thus reveal a novel mechanism whereby actin-associated proteins regulate proliferation by mediating the endocytosis and transportation of components in the canonical Wnt pathway. Moreover, the Fmn2-dependent signaling in this pathway parallels that seen in the non-canonical Wnt-dependent regulation of planar cell polarity through the Formin homology protein Daam. These studies provide evidence for integration of actin-associated processes in directing neuroepithelial proliferation.

Citace poskytuje Crossref.org

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