title: The unique mechanism of SNX9 BAR domain for inducing membrane tubulation.
abstract: Sorting nexin 9 (SNX9) is a member of the sorting nexin family of proteins and plays a critical role in clathrin-mediated endocytosis. It has a Bin-Amphiphysin-Rvs (BAR) domain which can form a crescent-shaped homodimer structure that induces deformation of the plasma membrane. While other BAR-domain containing proteins such as amphiphysin and endophilin have an amphiphatic helix in front of the BAR domain which plays a critical role in membrane penetration, SNX9 does not. Thus, whether and how SNX9 BAR domain could induce the deformation of the plasma membrane is not clear. The present study identified the internal putative amphiphatic stretch in the 1(st) α-helix of the SNX9 BAR domain and proved that together with the N-terminal helix (H0) region, this internal putative amphiphatic stretch is critical for inducing membrane tubulation. Therefore, our study shows that SNX9 uses a unique mechanism to induce the tubulation of the plasma membrane which mediates proper membrane deformation during clathrin-mediated endocytosis.
authors.affiliation: Department of Physiology and Biomedical Sciences, Seoul National University College of Medicine, Seoul 110-799, Korea ; Biomembrane Plasticity Research Center, Seoul National University College of Medicine, Seoul 110-799, Korea.
authors.forename: Joohyun
authors.initials: J
authors.lastname: Park
authors.affiliation: Department of Physiology and Biomedical Sciences, Seoul National University College of Medicine, Seoul 110-799, Korea.
authors.forename: Haiyan
authors.initials: H
authors.lastname: Zhao
authors.affiliation: Department of Physiology and Biomedical Sciences, Seoul National University College of Medicine, Seoul 110-799, Korea ; Biomembrane Plasticity Research Center, Seoul National University College of Medicine, Seoul 110-799, Korea.
authors.forename: Sunghoe
authors.initials: S
authors.lastname: Chang
mesh_terms: D048868:Adaptor Proteins, Signal Transducing / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D019556:COS Cells; D002462:Cell Membrane / Q000378:metabolism*; D002522:Chlorocebus aethiops; D002966:Clathrin / Q000378:metabolism; D004705:Endocytosis; D057809:HEK293 Cells; D006801:Humans; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009419:Nerve Tissue Proteins / Q000378:metabolism; D017434:Protein Structure, Tertiary / Q000235:genetics; D058305:Sorting Nexins / Q000235:genetics / Q000378:metabolism*
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D002966:Clathrin; D009419:Nerve Tissue Proteins; C107640:SH3GL2 protein, human; C400533:SNX9 protein, human; D058305:Sorting Nexins; C075637:amphiphysin
keywords: BAR domain; amphiphatic helix; clathrin-mediated endocytosis; invagination; tubulation