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SEC13 Sec13p

Sec13, Sec13p
The protein encoded by this gene belongs to the SEC13 family of WD-repeat proteins. It is a constituent of the endoplasmic reticulum and the nuclear pore complex. It has similarity to the yeast SEC13 protein, which is required for vesicle biogenesis from endoplasmic reticulum during the transport of proteins. Multiple alternatively spliced transcript variants have been found. [provided by RefSeq, Oct 2008] (from NCBI)
Top mentioned proteins: CAN, ACID, CD45, sec12, COPI
Papers on Sec13
A microtubule-independent role of p150glued in secretory cargo concentration at endoplasmic reticulum exit sites.
Weiss et al., Heidelberg, Germany. In J Cell Sci, Dec 2015
Assembly of the COPII coat complex, which occurs at ER exit sites (ERES), is initiated by membrane association and GTP loading of SAR1, followed by the recruitment of the SEC23-SEC24 and SEC13-SEC31 subcomplexes.
Regulation of mTORC1 by PI3K signaling.
Cantley et al., Boston, United States. In Trends Cell Biol, Sep 2015
Activation of mTORC1 [composed of mTOR, regulatory-associated protein of mTOR (Raptor), mammalian lethal with SEC13 protein 8(mLST8), 40-kDa proline-rich Akt substrate (PRAS40), and DEP domain-containing mTOR-interacting protein (DEPTOR)] depends on the Ras-related GTPases (Rags) and Ras homolog enriched in brain (Rheb) GTPase and requires signals from amino acids, glucose, oxygen, energy (ATP), and growth factors (including cytokines and hormones such as insulin).
Traffic of p24 Proteins and COPII Coat Composition Mutually Influence Membrane Scaffolding.
Miller et al., New York City, United States. In Curr Biol, Jun 2015
The Sec13p subunit of the COPII coat contributes to membrane scaffolding, which enforces curvature on the nascent vesicle.
Identification of novel genes involved in gastric carcinogenesis by suppression subtractive hybridization.
Setayesh et al., Tehrān, Iran. In Hum Exp Toxicol, 2015
The genes were ribosomal protein L18A, RNase H2 subunit B, SEC13, eukaryotic translation initiation factor 4A1, tetraspanin 8, cytochrome c oxidase subunit 2, NADH dehydrogenase subunit 4, and mitochondrially encoded ATP synthase 6.
Identification and characterization of novel factors that act in the nonsense-mediated mRNA decay pathway in nematodes, flies and mammals.
Cáceres et al., Brighton, United Kingdom. In Embo Rep, 2015
Two of their human homologs, GNL2 (ngp-1) and SEC13 (npp-20), are also required for NMD in human cells.
Comprehensive identification of host modulators of HIV-1 replication using multiple orthologous RNAi reagents.
Brass et al., Boston, United States. In Cell Rep, 2014
We further investigated the roles of GOLGI49, SEC13, and COG in HIV-1 replication.
The nuclear pore complex function of Sec13 protein is required for cell survival during retinal development.
Peng et al., Key West, United States. In J Biol Chem, 2014
Sec13 is a dual function protein, being a core component of both the COPII coat, which mediates protein trafficking from the endoplasmic reticulum to the Golgi apparatus, and the nuclear pore complex (NPC), which facilitates nucleo-cytoplasmic traffic.
MAIGO5 functions in protein export from Golgi-associated endoplasmic reticulum exit sites in Arabidopsis.
Hara-Nishimura et al., Kyoto, Japan. In Plant Cell, 2013
Coat protein complex II (COPII) components, which include two heterodimers of Secretory23/24 (Sec23/24) and Sec13/31, facilitate selective cargo export from the ER; however, little is known about the mechanisms that regulate their recruitment to the ER membrane, especially in plants.
Sit4p/PP6 regulates ER-to-Golgi traffic by controlling the dephosphorylation of COPII coat subunits.
Ferro-Novick et al., San Diego, United States. In Mol Biol Cell, 2013
The coat inner shell recruits the Sec13p-Sec31p complex, leading to coat polymerization and vesicle budding.
mTOR kinase structure, mechanism and regulation.
Pavletich et al., New York City, United States. In Nature, 2013
Here we report co-crystal structures of a complex of truncated mTOR and mammalian lethal with SEC13 protein 8 (mLST8) with an ATP transition state mimic and with ATP-site inhibitors.
SEC23B is required for the maintenance of murine professional secretory tissues.
Zhang et al., Cleveland, United States. In Proc Natl Acad Sci U S A, 2012
COPII contains five core components: SAR1, SEC23, SEC24, SEC13, and SEC31.
ER cargo properties specify a requirement for COPII coat rigidity mediated by Sec13p.
Miller et al., New York City, United States. In Science, 2012
Sec13p may rigidify the COPII cage and increase its membrane-bending capacity
Epithelial organization and cyst lumen expansion require efficient Sec13-Sec31-driven secretion.
Stephens et al., Bristol, United Kingdom. In J Cell Sci, 2012
When embedded in a three-dimensional matrix, Sec13-depleted Caco-2 cells form cysts but, unlike controls, are defective in lumen expansion.
A conserved coatomer-related complex containing Sec13 and Seh1 dynamically associates with the vacuole in Saccharomyces cerevisiae.
Dargemont et al., Paris, France. In Mol Cell Proteomics, 2011
Here, we identify the Seh1-associated protein complex in yeast that contains the nucleoporins Seh1 and Sec13
Molecular architecture of the Nup84-Nup145C-Sec13 edge element in the nuclear pore complex lattice.
Schwartz et al., Cambridge, United States. In Nat Struct Mol Biol, 2009
The heterotypic ACE1 interaction of Nup84 and Nup145C is analogous to the homotypic ACE1 interaction of Sec31 that forms COPII lattice edge elements and is inconsistent with the alternative 'fence-like' NPC model.
Structure of a trimeric nucleoporin complex reveals alternate oligomerization states.
Hoelz et al., New York City, United States. In Proc Natl Acad Sci U S A, 2009
crystal structure of the heterotrimeric Sec13 x Nup145C x Nup84 complex, centerpiece of the heptamer, at 3.2-A resolution. Nup84 forms a U-shaped alpha-helical solenoid domain, topologically similar to two other members of the heptamer, Nup145C and Nup85
A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores.
Hurt et al., Heidelberg, Germany. In Cell, 1996
Nup84p forms a complex with five proteins, of which Nup120p, Nup85p, Sec13p, and a Sec13p homolog were identified.
COPI- and COPII-coated vesicles bud directly from the endoplasmic reticulum in yeast.
Orci et al., Berkeley, United States. In Cell, 1996
The cytosolic yeast proteins Sec13p-Sec31p, Sec23p-Sec24p, and the small GTP-binding protein Sar1p generate protein transport vesicles by forming the membrane coat termed COPII.
COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum.
Schekman et al., Berkeley, United States. In Cell, 1994
In vitro synthesis of endoplasmic reticulum-derived transport vesicles has been reconstituted with washed membranes and three soluble proteins (Sar1p, Sec13p complex, and Sec23p complex).
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