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. 2010 Nov 15;21(22):3973–3984. doi: 10.1091/mbc.E10-03-0261

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© 2010 by The American Society for Cell Biology

This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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Scheme 1. — Model of CNN3-dependent trophoblast fusion (I) In unstimulated cells, CNN3 is constitutively phosphorylated at Ser293 and Ser296 in the regulatory tail and is associated with F-actin cytoskeleton via actin-binding sites. (II) When cells receive a fusion signal, factor (or signal) “X” is induced/activated and binds to (or recognizes) the phosphorylated regulatory tail and triggered CNN3 dissociation from actin. The phosphomimetic S293/296D mutant responds to the signal, while ΔC and S293/296A are unresponsive and remain attached to F-actin. (III) After CNN3 release, actin bundles are rearranged and then disappeared. (IV) Released CNN3 is dephosphorylated or degradaded in cytoplasm.