Actin polymerization promotes invagination of flat clathrin-coated lattices in mammalian cells by pushing at lattice edges

Changsong Yang, Patricia Colosi, Siewert Hugelier, Daniel Zabezhinsky, Melike Lakadamyali and Tatyana Svitkina ()
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Changsong Yang: University of Pennsylvania
Patricia Colosi: University of Pennsylvania
Siewert Hugelier: University of Pennsylvania
Daniel Zabezhinsky: University of Pennsylvania
Melike Lakadamyali: University of Pennsylvania
Tatyana Svitkina: University of Pennsylvania

Nature Communications, 2022, vol. 13, issue 1, 1-20

Abstract: Abstract Clathrin-mediated endocytosis (CME) requires energy input from actin polymerization in mechanically challenging conditions. The roles of actin in CME are poorly understood due to inadequate knowledge of actin organization at clathrin-coated structures (CCSs). Using platinum replica electron microscopy of mammalian cells, we show that Arp2/3 complex-dependent branched actin networks, which often emerge from microtubule tips, assemble along the CCS perimeter, lack interaction with the apical clathrin lattice, and have barbed ends oriented toward the CCS. This structure is hardly compatible with the widely held “apical pulling” model describing actin functions in CME. Arp2/3 complex inhibition or epsin knockout produce large flat non-dynamic CCSs, which split into invaginating subdomains upon recovery from Arp2/3 inhibition. Moreover, epsin localization to CCSs depends on Arp2/3 activity. We propose an “edge pushing” model for CME, wherein branched actin polymerization promotes severing and invagination of flat CCSs in an epsin-dependent manner by pushing at the CCS boundary, thus releasing forces opposing the intrinsic curvature of clathrin lattices.

Date: 2022
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DOI: 10.1038/s41467-022-33852-2

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