Abstract：
:Multiple proteins act co-operatively in mammalian clathrin-mediated endocytosis (CME) to generate endocytic vesicles from the plasma membrane. The principles controlling the activation and organization of the actin cytoskeleton during mammalian CME are, however, not fully understood. Here, we show that the protein FCHSD2 is a major activator of actin polymerization during CME. FCHSD2 deletion leads to decreased ligand uptake caused by slowed pit maturation. FCHSD2 is recruited to endocytic pits by the scaffold protein intersectin via an unusual SH3-SH3 interaction. Here, its flat F-BAR domain binds to the planar region of the plasma membrane surrounding the developing pit forming an annulus. When bound to the membrane, FCHSD2 activates actin polymerization by a mechanism that combines oligomerization and recruitment of N-WASP to PI(4,5)P2, thus promoting pit maturation. Our data therefore describe a molecular mechanism for linking spatiotemporally the plasma membrane to a force-generating actin platform guiding endocytic vesicle maturation.
journal_name
Celljournal_title
Cellauthors
Almeida-Souza L,Frank RAW,García-Nafría J,Colussi A,Gunawardana N,Johnson CM,Yu M,Howard G,Andrews B,Vallis Y,McMahon HTdoi
10.1016/j.cell.2018.05.020subject
Has Abstractpub_date
2018-07-12 00:00:00pages
325-337.e14issue
2eissn
0092-8674issn
1097-4172pii
S0092-8674(18)30597-Xjournal_volume
174pub_type
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