Synergies between Aip1p and capping protein subunits (Acp1p and Acp2p) in clathrin-mediated endocytosis and cell polarization in fission yeast.

Aip1p cooperates with ADF/cofilin to disassemble actin filaments in vitro and in vivo, and is proposed to cap actin filament barbed ends. In this paper, we address the synergies between Aip1p and the capping protein heterodimer, Acp1p/Acp2p, during clathrin-mediated endocytosis in fission yeast. Using quantitative microscopy and new methods for ...
data alignment and analysis (Berro and Pollard, 2014) we show that heterodimeric capping protein can replace Aip1p, but Aip1p cannot replace capping protein in endocytic patches. Our quantitative analysis reveals that the actin meshwork is organized radially and is compacted by the crosslinker fimbrin before the endocytic vesicle is released from the plasma membrane. Capping protein and Aip1p help maintain the high density of actin filaments in meshwork by keeping actin filaments close enough for crosslinking. Our experiments also reveal new cellular functions for Acp1p and Acp2p independent from their capping activity. We identified two independent pathways that control polarization of endocytic sites, one depending on acp2+ and aip1+ during interphase and the other independent of acp1+, acp2+ and aip1+ during mitosis.
Mol. Biol. Cell
Date: Aug. 20, 2014
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