Reactome: A Curated Pathway Database

F- and N- BAR domain proteins bind the clathrin-coated pit

Stable Identifier
Homo sapiens
Locations in the PathwayBrowser

BAR (BIN/amphiphysin/Rvs) domain proteins sense and contribute to membrane curvature. BAR domain proteins generally form long, coiled-coil homo- or hetero-dimers with a concave inner surface that interacts with membranes (reviewed in Gallop and McMahon, 2005; Daumke et al, 2014). F-BAR domain proteins such as FCHo 1 and 2 recognize shallow membrane curvature and are generally recruited early in the formation of clathrin-coated pit (Itoh et al, 2005; Kamioka et al, 2004; Henne et al, 2007; Shimada et al, 2007; Henne et al, 2010). FNBP proteins and N-BAR containing endocytic proteins such as SNX9 and 18, amphiphysin (AMPH) and endophilins recognize regions of membrane with greater curvature, interact with dynamin and likely play a later role in CCP formation with spatiotemporal coupling to vesicle scission (Kamioka et al, 2004; Itoh et al, 2005; Soulet et al, 2005; Shimada et al, 2007; Shin et al, 2008; Taylor et al, 2011; reveiwed in McMahon and Boucrot, 2011). These proteins are recruited to the complex through interactions with core components of the clathrin-coated pit, and in the case of SNX9, also through interaction with PI(3,4)P2, which is generated at late stages by clathrin-associated PIK3C2A (Lundmark and Carlson, 2003; Schmid et al, 2006; Dergai et al, 2010; Brett et al, 2002 : Posor et al, 2013; reviewed in Daumke et al, 2014). Early BAR domain containing proteins such as FCHo1 and 2 are not present in either late stage clathrin-coated pits or in free clathrin-coated vesicles. Although the precise timing of their dissociation is not known, in this pathway, they are shown leaving the clathrin-coated pit upon recruitment of the more highly curved N-BAR proteins (Taylor et al, 2011).

Literature References
PubMed ID Title Journal Year
17540576 Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature Structure 2007
17512409 Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis Cell 2007
21779028 Molecular mechanism and physiological functions of clathrin-mediated endocytosis Nat. Rev. Mol. Cell Biol. 2011
15703209 SNX9 regulates dynamin assembly and is required for efficient clathrin-mediated endocytosis Mol. Biol. Cell 2005
23823722 Spatiotemporal control of endocytosis by phosphatidylinositol-3,4-bisphosphate Nature 2013
16903783 Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly PLoS Biol. 2006
20448150 FCHo proteins are nucleators of clathrin-mediated endocytosis Science 2010
16326391 Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins Dev. Cell 2005
12057195 Accessory protein recruitment motifs in clathrin-mediated endocytosis Structure 2002
15649145 BAR domains and membrane curvature: bringing your curves to the BAR Biochem. Soc. Symp. 2005
12952949 Sorting nexin 9 participates in clathrin-mediated endocytosis through interactions with the core components J. Biol. Chem. 2003
20946875 Intersectin 1 forms complexes with SGIP1 and Reps1 in clathrin-coated pits Biochem. Biophys. Res. Commun. 2010
24581490 BAR domain scaffolds in dynamin-mediated membrane fission Cell 2014
21445324 A high precision survey of the molecular dynamics of mammalian clathrin-mediated endocytosis PLoS Biol. 2011
15252009 A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis J. Biol. Chem. 2004
18388313 SNX9 regulates tubular invagination of the plasma membrane through interaction with actin cytoskeleton and dynamin 2 J. Cell. Sci. 2008
Participant Of
This entity is regulated by:
Orthologous Events