Wnt5a directs polarized calcium gradients by recruiting cortical endoplasmic reticulum to the cell trailing edge.

Wnt5a directs polarized calcium gradients by recruiting cortical endoplasmic reticulum to the cell trailing edge.
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DOI:
10.1016/j.devcel.2013.08.019
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发表时间:
2013-09-30
期刊:
影响因子:
11.8
通讯作者:
Ahn, Natalie G.
Ahn, Natalie G.
中科院分区:
生物学1区
文献类型:
--
作者:
Witze, Eric S.;Connacher, Mary Katherine;Houel, Stephane;Schwartz, Michael P.;Morphew, Mary K.;Reid, Leah;Sacks, David B.;Anseth, Kristi S.;Ahn, Natalie G.

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Wnt5a directs the assembly of “Wnt-receptor-actin-myosin-polarity (WRAMP)” structure, which integrates cell adhesion receptors with F-actin and myosin to form a microfilament array associated with multivesicular bodies. The WRAMP structure is polarized to the cell posterior, where it directs tail-end membrane retraction, driving forward translocation of the cell body. Here, we define constituents of the WRAMP proteome, including regulators of microfilament and microtubule dynamics, protein interactions, and enzymatic activity. IQGAP1, a scaffold for F-actin nucleation and crosslinking, is necessary for WRAMP structure formation, potentially bridging microfilaments and MVBs. Vesicle coat proteins, including coatomer-I subunits, localize to and are required for the WRAMP structure. Electron microscopy and live imaging demonstrate movement of ER to the WRAMP structure and plasma membrane, followed by elevation of intracellular Ca2+. Thus, Wnt5a controls directional movement by recruiting cortical ER to mobilize a rear-directed, localized Ca2+ signal, activating actomyosin contraction and adhesion disassembly for membrane retraction.
DIA1和IQGAP1在细胞迁移和吞噬杯形成中相互作用。
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