F-BAR domain only protein 2

Definition:

Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a lipid-binding activity with a preference for membranes enriched in phosphatidylserine and phosphoinositides (Pi(4,5) biphosphate) like the plasma membrane. Its membrane-bending activity might be important for the subsequent action of clathrin and adaptors in the formation of clathrin-coated vesicles. Involved in adaptor protein complex AP-2-dependent endocytosis of the transferrin receptor, it also functions in the AP-2-independent endocytosis of the LDL receptor.

References:

[1]. Akiyoshi Uezu, et al. Characterization of the EFC/F-BAR domain protein, FCHO2. Genes Cells. 2011 Aug;16(8):868-78. [Content Brief]

[2]. William Mike Henne, et al. FCHo proteins are nucleators of clathrin-mediated endocytosis. Science. 2010 Jun 4;328(5983):1281-4. [Content Brief]

[3]. William Mike Henne, et al. Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature. Structure. 2007 Jul;15(7):839-52. [Content Brief]

[4]. Erin E Mulkearns, et al. FCH domain only-2 organizes clathrin-coated structures and interacts with Disabled-2 for low-density lipoprotein receptor endocytosis. Mol Biol Cell. 2012 Apr;23(7):1330-42. [Content Brief]

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