Expression and properties of sorting nexin 9 in dynamin-mediated endocytosis.
Sorting nexin 9 (SNX9) is identified as an important regulator of dynamin function in clathrin-mediated endocytosis. SNX9 recruits dynamin to the plasma membrane and promotes its GTPase activity, resulting in membrane constriction and ultimate transport vesicle scission. This chapter describes procedures to express recombinant SNX9, to biochemically characterize the cytosolic complex between SNX9 and dynamin, and to identify additional interacting partners of SNX9. Assays are presented to investigate the requirements for SNX9-dependent membrane recruitment of dynamin in vitro and in vivo.
Lundmark
Richard
R
Department of Medical Biochemistry and Biophysics, Umeå University, Sweden.
Carlsson
Sven R
SR
D002352:Carrier Proteins / Q000096:biosynthesis* / Q000502:physiology*; D003600:Cytosol / Q000378:metabolism; D034281:Dynamins / Q000502:physiology*; D004705:Endocytosis / Q000502:physiology*; D005982:Glutathione Transferase / Q000235:genetics; D006801:Humans; D020014:K562 Cells; D008081:Liposomes / Q000378:metabolism; D025941:Protein Interaction Mapping; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis; D058305:Sorting Nexins; D033921:Vesicular Transport Proteins
D002352:Carrier Proteins; D008081:Liposomes; D011993:Recombinant Fusion Proteins; C400533:SNX9 protein, human; D058305:Sorting Nexins; D033921:Vesicular Transport Proteins; D005982:Glutathione Transferase; D034281:Dynamins