BAR domain proteins recruit dynamin

Stable Identifier
R-HSA-8868236
Type
Reaction
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
Summation

Dynamin is a large GTPase whose GTP hydrolysis activity is required for the scission of clathrin-coated vesicles from the plasma membrane (reviewed in Ferguson and De Camilli, 2012). Dynamin is recruited to the plasma membrane through protein-protein interactions with many components of the clathrin-coated pit including ITSNs, SNX9 and 18 and amphiphysin (Lundmark and Carlsson, 2003; Soulet et al, 2005; David et al, 1996; Owen et al, 1998; Shupliakov et al, 1997). Although dynamin is recruited at lower levels throughout formation of the clathrin-coated pit, the bulk of dynamin is recruited at late stages, after the incorporation of BAR domain-containing proteins and actin-polymerizing factors (Ferguson et al, 2009; Taylor et al, 2011; Taylor et al, 2012; Posor et al, 2013; Meineke et al, 2013; Aguet et al, 2013; reviewed in Daumke et al, 2014). Several BAR domain proteins have SH3 domains that bind the proline rich domain (PRD) of dynamin. These interactions regulate dynamin GTPsae activity and vesicle formation (Neuman and Schmid, 2013). To facilitate scission of a clathrin-coated pit from the plasma membrane, dynamin self assembles into helical oligomers, stimulating its GTPase activity and contributing to the membrane remodeling required to form the neck of the emerging vesicle (Sweitzer and Hinshaw 1998; Yoshida et al, 2004; Chappie et al, 2010; Faelber et al, 2011; Ford et al, 2011; reviewed in McMahon and Boucrot, 2011; Daumke et al, 2014).

Literature References
PubMed ID Title Journal Year
9736607 Crystal structure of the amphiphysin-2 SH3 domain and its role in the prevention of dynamin ring formation EMBO J. 1998
21779028 Molecular mechanism and physiological functions of clathrin-mediated endocytosis Nat. Rev. Mol. Cell Biol. 2011
21927001 The crystal structure of dynamin Nature 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
8552632 A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals Proc. Natl. Acad. Sci. U.S.A. 1996
20428113 G domain dimerization controls dynamin's assembly-stimulated GTPase activity Nature 2010
23297414 Cooperative recruitment of dynamin and BIN/amphiphysin/Rvs (BAR) domain-containing proteins leads to GTP-dependent membrane scission J. Biol. Chem. 2013
9092476 Synaptic vesicle endocytosis impaired by disruption of dynamin-SH3 domain interactions Science 1997
23861397 Dual role of BAR domain-containing proteins in regulating vesicle release catalyzed by the GTPase, dynamin-2 J. Biol. Chem. 2013
20059951 Coordinated actions of actin and BAR proteins upstream of dynamin at endocytic clathrin-coated pits Dev. Cell 2009
23891661 Advances in analysis of low signal-to-noise images link dynamin and AP2 to the functions of an endocytic checkpoint Dev. Cell 2013
12952949 Sorting nexin 9 participates in clathrin-mediated endocytosis through interactions with the core components J. Biol. Chem. 2003
24581490 BAR domain scaffolds in dynamin-mediated membrane fission Cell 2014
21927000 Crystal structure of nucleotide-free dynamin Nature 2011
15318165 The stimulatory action of amphiphysin on dynamin function is dependent on lipid bilayer curvature EMBO J. 2004
22505844 A feedback loop between dynamin and actin recruitment during clathrin-mediated endocytosis PLoS Biol. 2012
21445324 A high precision survey of the molecular dynamics of mammalian clathrin-mediated endocytosis PLoS Biol. 2011
9635431 Dynamin undergoes a GTP-dependent conformational change causing vesiculation Cell 1998
22233676 Dynamin, a membrane-remodelling GTPase Nat. Rev. Mol. Cell Biol. 2012
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