FCHo Proteins Are Nucleators of Clathrin-Mediated Endocytosms.

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Bibliographic Details
Title:	FCHo Proteins Are Nucleators of Clathrin-Mediated Endocytosms.
Authors:	Henne, William Mike, Boucrot, Emmanuel, Meinecke, Michael, Evergren, Emma, Vallis, Yvonne, Mittal, Rohit, McMahon, Harvey T.
Source:	Science (pre-March 2025). 6/4/2010, Vol. 328 Issue 5983, p1281-1284. 4p.
Subjects:	Endocytosis, Protein research, Ligands (Chemistry), Eukaryotic cells, Gene expression, Synaptic vesicles
Abstract:	Clathrin-mediated endocytosis, the major pathway for ligand internalization into eukaryotic cells, is thought to be initiated by the clustering of clathrin and adaptors around receptors destined for internalization. However, here we report that the membrane-sculpting F-BAR domain-containing Fer/Cip4 homotogy domain-only proteins 1 and 2 (FCHol/2) were required for plasma membrane clathrin-coated vesicle (CCV) budding and marked sites of CCV formation. Changes in FCHol/2 expression levels correlated directly with numbers of CCV budding events, ligand endocytosis, and synaptic vesicle marker recycling. FCHol/2 proteins bound specifically to the plasma membrane and recruited the scaffold proteins epsl5 and intersectin, which in turn engaged the adaptor complex AP2. The FCHo F-BAR membrane-bending activity was required, leading to the proposal that FCHol/2 sculpt the initial bud site and recruit the clathrin machinery for CCV formation. [ABSTRACT FROM AUTHOR]
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Database:	Psychology and Behavioral Sciences Collection

Description
Abstract:	Clathrin-mediated endocytosis, the major pathway for ligand internalization into eukaryotic cells, is thought to be initiated by the clustering of clathrin and adaptors around receptors destined for internalization. However, here we report that the membrane-sculpting F-BAR domain-containing Fer/Cip4 homotogy domain-only proteins 1 and 2 (FCHol/2) were required for plasma membrane clathrin-coated vesicle (CCV) budding and marked sites of CCV formation. Changes in FCHol/2 expression levels correlated directly with numbers of CCV budding events, ligand endocytosis, and synaptic vesicle marker recycling. FCHol/2 proteins bound specifically to the plasma membrane and recruited the scaffold proteins epsl5 and intersectin, which in turn engaged the adaptor complex AP2. The FCHo F-BAR membrane-bending activity was required, leading to the proposal that FCHol/2 sculpt the initial bud site and recruit the clathrin machinery for CCV formation. [ABSTRACT FROM AUTHOR]
ISSN:	00368075
DOI:	10.1126/science.1188462