title: A conserved coatomer-related complex containing Sec13 and Seh1 dynamically associates with the vacuole in Saccharomyces cerevisiae.
abstract: The presence of multiple membrane-bound intracellular compartments is a major feature of eukaryotic cells. Many of the proteins required for formation and maintenance of these compartments share an evolutionary history. Here, we identify the SEA (Seh1-associated) protein complex in yeast that contains the nucleoporin Seh1 and Sec13, the latter subunit of both the nuclear pore complex and the COPII coating complex. The SEA complex also contains Npr2 and Npr3 proteins (upstream regulators of TORC1 kinase) and four previously uncharacterized proteins (Sea1-Sea4). Combined computational and biochemical approaches indicate that the SEA complex proteins possess structural characteristics similar to the membrane coating complexes COPI, COPII, the nuclear pore complex, and, in particular, the related Vps class C vesicle tethering complexes HOPS and CORVET. The SEA complex dynamically associates with the vacuole in vivo. Genetic assays indicate a role for the SEA complex in intracellular trafficking, amino acid biogenesis, and response to nitrogen starvation. These data demonstrate that the SEA complex is an additional member of a family of membrane coating and vesicle tethering assemblies, extending the repertoire of protocoatomer-related complexes.
authors: Institut Jacques Monod, CNRS UMR 7592, Bâtiment Buffon, Paris, France. svetlana.dokudovskaya@igr.fr
authors: Svetlana
authors: S
authors: Dokudovskaya
authors: Francois
authors: F
authors: Waharte
authors: Avner
authors: A
authors: Schlessinger
authors: Ursula
authors: U
authors: Pieper
authors: Damien P
authors: DP
authors: Devos
authors: Ileana M
authors: IM
authors: Cristea
authors: Rosemary
authors: R
authors: Williams
authors: Jean
authors: J
authors: Salamero
authors: Brian T
authors: BT
authors: Chait
authors: Andrej
authors: A
authors: Sali
authors: Mark C
authors: MC
authors: Field
authors: Michael P
authors: MP
authors: Rout
authors: Catherine
authors: C
authors: Dargemont
mesh_terms: D001343:Autophagy; D047468:Immunoprecipitation; D007425:Intracellular Membranes / Q000378:metabolism; D008958:Models, Molecular; D046912:Multiprotein Complexes / Q000378:metabolism; D028861:Nuclear Pore Complex Proteins / Q000737:chemistry / Q000378:metabolism*; D010641:Phenotype; D010802:Phylogeny; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D021381:Protein Transport; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism*; D040681:Structural Homology, Protein; D013347:Subcellular Fractions / Q000378:metabolism; D014617:Vacuoles / Q000378:metabolism*
chemical_list: D046912:Multiprotein Complexes; D028861:Nuclear Pore Complex Proteins; C079620:SEC13 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; C533526:Seh1 protein, S cerevisiae