Link to bioRxiv paper:
http://biorxiv.org/cgi/content/short/2022.11.21.517438v1?rss=1

Authors: Yu, Y., Ozaki, T., Yoshimura, S. H.

Abstract:
Clathrin-mediated endocytosis plays a pivotal role in signal transduction pathways between the extracellular environment and the intracellular space. Accumulating evidence from live-cell imaging and super-resolution microscopy of mammalian cells suggests an asymmetric distribution of actin fibers near the clathrin-coated pit, which induces asymmetric pit-closing, rather than radial constriction. However, detailed molecular mechanisms of this asymmetricity remain elusive. Herein, we used high-speed atomic force microscopy to demonstrate that CIP4, a multidomain protein with a classic F-BAR domain and intrinsically disordered regions, is necessary for asymmetric pit-closing. Strong self-assembly of CIP4 via intrinsically disordered regions, together with stereospecific interactions with the curved membrane and actin-regulating proteins, generates a small actin-rich environment near the pit, which deforms the membrane and closes the pit. Our results provide a mechanistic insight into how spatio-temporal actin polymerization near the plasma membrane is promoted by a collaboration of disordered and structured domains.

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