Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins.

By T. Itoh, K. S. Erdmann, Aurélien Roux, Bianca Habermann, H. Werner, P. De Camilli. Developmental Cell, 2005

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Dynamin, a membrane remodelling GTPase (2012, background): “, involves the recruitment of BAR domain-containing proteins, several of which bind dynamin as well as the PtdIns(4,5)P 2 phosphatase synaptojani”
Harnessing actin dynamics for clathrin-mediated endocytosis (2006, background): “Dynamin might also be linked to the actin cytoskeleton through a family of proteins that contain BAR or related F-BAR domains, which both bind to lipids and can tubulate membranes, potentially facilitating endocytosi”
A High Precision Survey of the Molecular Dynamics of Mammalian Clathrin-Mediated Endocytosis (2011, background): “Sequential Recruitment of Positive and Negative Regulators of Actin Polymerization It is generally accepted that actin polymerization plays a role in some (but not all, see [52,53]) forms of CME [9,11,18,44,46, 47,50,54].”
Membrane recognition by phospholipid-binding domains (2008, background): “The ∼320-amino-acid F-BAR domain shows some sequence similarity to BAR domains and shares their ability to tubulate membranes and bind acidic phospholipid”