Genomes and Genes
Gene Symbol: SEC63
Description: protein-transporting protein SEC63
Alias: PTL1, protein-transporting protein SEC63
Species: Saccharomyces cerevisiae S288c
- Deshaies R, Sanders S, Feldheim D, Schekman R. Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex. Nature. 1991;349:806-8 pubmed..Genetic selections uncovered three Saccharomyces cerevisiae genes (SEC61, SEC62 and SEC63), mutations in which block import of precursor proteins into the ER lumen in vivo and in vitro...
- Wittke S, Dunnwald M, Johnsson N. Sec62p, a component of the endoplasmic reticulum protein translocation machinery, contains multiple binding sites for the Sec-complex. Mol Biol Cell. 2000;11:3859-71 pubmed..The C-terminal binding site of Sec62p is less important for complex stability, but adjoins the region in Sec62p that might be involved in signal sequence recognition. ..
- Jermy A, Willer M, Davis E, Wilkinson B, Stirling C. The Brl domain in Sec63p is required for assembly of functional endoplasmic reticulum translocons. J Biol Chem. 2006;281:7899-906 pubmed..Our data indicate that the SEC' complex is required for co-translational protein translocation across the yeast ER membrane. ..
- Willer M, Jermy A, Young B, Stirling C. Identification of novel protein-protein interactions at the cytosolic surface of the Sec63 complex in the yeast ER membrane. Yeast. 2003;20:133-48 pubmed..Finally, we determine the authentic N-terminus of Sec62p and describe interacting subdomains of both Sec62p and Sec63p. ..
- Ng D, Walter P. ER membrane protein complex required for nuclear fusion. J Cell Biol. 1996;132:499-509 pubmed..We have isolated novel sec63 mutant alleles that display severe karyogamy defects...
- Kabani M, Beckerich J, Gaillardin C. Sls1p stimulates Sec63p-mediated activation of Kar2p in a conformation-dependent manner in the yeast endoplasmic reticulum. Mol Cell Biol. 2000;20:6923-34 pubmed..Synthetic lethality was observed between DeltaScsls1 and translocation-deficient kar2 or sec63-1 mutants, providing in vivo evidence for a role of ScSls1p in protein translocation...
- McClellan A, Endres J, Vogel J, Palazzi D, Rose M, Brodsky J. Specific molecular chaperone interactions and an ATP-dependent conformational change are required during posttranslational protein translocation into the yeast ER. Mol Biol Cell. 1998;9:3533-45 pubmed..We conclude that a conformation- and ATP-dependent interaction of BiP with the J domain of Sec63p is essential for protein translocation and that the specificity of hsc70 action is dictated by their DnaJ partners. ..
- Wittke S, Lewke N, Muller S, Johnsson N. Probing the molecular environment of membrane proteins in vivo. Mol Biol Cell. 1999;10:2519-30 pubmed..The efficiency of the Nub and Cub reassembly to the quasi-native Ub reflects the proximity between Sec63-Cub and the Nub-labeled proteins...
- Römisch K. Surfing the Sec61 channel: bidirectional protein translocation across the ER membrane. J Cell Sci. 1999;112 ( Pt 23):4185-91 pubmed..Retrograde transport of soluble proteins through the Sec61 channel after signal-peptide cleavage, however, must be mechanistically distinct from signal-peptide-mediated import into the ER through the same channel. ..
- Harada Y, Li H, Wall J, Li H, Lennarz W. Structural studies and the assembly of the heptameric post-translational translocon complex. J Biol Chem. 2011;286:2956-65 pubmed publisher..the heptameric complex into three subcomplexes identified as the trimeric translocon Sec61-Sbh1-Sss1, the Sec63-Sec71-Sec72 trimer, and the heterotetramer Sec62-Sec63-Sec71-Sec72, respectively...
- Matlack K, Plath K, Misselwitz B, Rapoport T. Protein transport by purified yeast Sec complex and Kar2p without membranes. Science. 1997;277:938-41 pubmed..Movement through the channel occurred in detergent solution in the absence of a lipid bilayer. ..
- Ast T, Michaelis S, Schuldiner M. The Protease Ste24 Clears Clogged Translocons. Cell. 2016;164:103-114 pubmed publisher..These results shed light on a new and critical task of Ste24, which safeguards the essential process of translocation. ..
- Wilson J, Barlowe C. Yet1p and Yet3p, the yeast homologs of BAP29 and BAP31, interact with the endoplasmic reticulum translocation apparatus and are required for inositol prototrophy. J Biol Chem. 2010;285:18252-61 pubmed publisher..We propose a model for the Yet-Sec complex interaction that places Yet1p and Yet3p at the translocation pore to manage biogenesis of specific transmembrane secretory proteins. ..
- Young B, Craven R, Reid P, Willer M, Stirling C. Sec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo. EMBO J. 2001;20:262-71 pubmed..Here we demonstrate that Sec63p and Kar2p are also required for the SRP-dependent targeting pathway in vivo. Furthermore, we demonstrate multiple roles for Sec63p, at least one of which is exclusive to the SRP-independent pathway. ..
- Corsi A, Schekman R. The lumenal domain of Sec63p stimulates the ATPase activity of BiP and mediates BiP recruitment to the translocon in Saccharomyces cerevisiae. J Cell Biol. 1997;137:1483-93 pubmed
- Tafelmeyer P, Johnsson N, Johnsson K. Transforming a (beta/alpha)8--barrel enzyme into a split-protein sensor through directed evolution. Chem Biol. 2004;11:681-9 pubmed..This powerful selection complements the repertoire of the currently used split-protein sensors and provides a new tool for high-throughput interaction screening. ..
- Panzner S, Dreier L, Hartmann E, Kostka S, Rapoport T. Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p. Cell. 1995;81:561-70 pubmed..We therefore hypothesize that distinct membrane protein complexes function in co- and posttranslational translocation pathways. ..
- Piña F, O Donnell A, Pagant S, Piao H, Miller J, Fields S, et al. Hph1 and Hph2 are novel components of the Sec63/Sec62 posttranslational translocation complex that aid in vacuolar proton ATPase biogenesis. Eukaryot Cell. 2011;10:63-71 pubmed publisher..yeast two-hybrid screen and identified their interactions with Sec71, a subunit of the Sec63/Sec62 complex, which mediates posttranslational translocation of proteins into the ER...
- Rubenstein E, Kreft S, Greenblatt W, Swanson R, Hochstrasser M. Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase. J Cell Biol. 2012;197:761-73 pubmed publisher..Hrd1 therefore likely plays a general role in targeting proteins that persistently associate with and potentially obstruct the translocon. ..
- Müller L, de Escauriaza M, Lajoie P, Theis M, Jung M, Müller A, et al. Evolutionary gain of function for the ER membrane protein Sec62 from yeast to humans. Mol Biol Cell. 2010;21:691-703 pubmed publisher..similarity to their yeast orthologues, the two membrane proteins of the human endoplasmic reticulum (ER) Sec62 and Sec63 are expected to play a role in protein biogenesis in the ER...
- Sato K, Sato M, Nakano A. Rer1p as common machinery for the endoplasmic reticulum localization of membrane proteins. Proc Natl Acad Sci U S A. 1997;94:9693-8 pubmed..The Mfalpha1p fusions of Sec12p, Sec71p, and Sec63p were all more or less mislocalized in ret1-1. These observations imply that the roles of Rer1p and coatomer are much more general than thought before. ..
- Soromani C, Zeng N, Hollemeyer K, Heinzle E, Klein M, Tretter T, et al. N-acetylation and phosphorylation of Sec complex subunits in the ER membrane. BMC Cell Biol. 2012;13:34 pubmed publisher..Sec61 complex (Sec61p, Sbh1p, Sss1p) which on its own mediates cotranslational protein import into the ER and the Sec63 complex (Sec63p, Sec62p, Sec71p, Sec72p)...
- Loibl M, Wunderle L, Hutzler J, Schulz B, Aebi M, Strahl S. Protein O-mannosyltransferases associate with the translocon to modify translocating polypeptide chains. J Biol Chem. 2014;289:8599-611 pubmed publisher..We demonstrate the association of Pmt1-Pmt2 with the OST, the trimeric Sec61, and the tetrameric Sec63 complex in vivo by co-immunoprecipitation...
- Zhang W, Zhao H, Xue C, Xiong X, Yao X, Li X, et al. Enhanced secretion of heterologous proteins in Pichia pastoris following overexpression of Saccharomyces cerevisiae chaperone proteins. Biotechnol Prog. 2006;22:1090-5 pubmed..In the present study we evaluated the role of the chaperones Kar2p, Sec63, YDJ1p, Ssa1p, and PDI from Saccharomyces cerevisiae...
- Meiringer C, Rethmeier R, Auffarth K, Wilson J, Perz A, Barlowe C, et al. The Dsl1 protein tethering complex is a resident endoplasmic reticulum complex, which interacts with five soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptors (SNAREs): implications for fusion and fusion regulation. J Biol Chem. 2011;286:25039-46 pubmed publisher..Our data support a model, in which a tethering complex is stabilized at the organelle membrane by binding to SNAREs, recognizes the incoming vesicle via its coat and then promotes its SNARE-mediated fusion. ..
- Pilon M, Römisch K, Quach D, Schekman R. Sec61p serves multiple roles in secretory precursor binding and translocation into the endoplasmic reticulum membrane. Mol Biol Cell. 1998;9:3455-73 pubmed..Only mutants of the second class were partially suppressed by overexpression of SEC63, which encodes a subunit of the Sec61 holoenzyme complex responsible for positioning Kar2p (yeast BiP) at the ..
- Mutka S, Walter P. Multifaceted physiological response allows yeast to adapt to the loss of the signal recognition particle-dependent protein-targeting pathway. Mol Biol Cell. 2001;12:577-88 pubmed..Thus, we suggest that cells trade speed in cell growth for fidelity in protein sorting to adjust to life without SRP. ..