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SEC61 Sec61p

Sec61, Sec61p, Sec61alpha
The protein encoded by this gene belongs to the SECY/SEC61- alpha family. It appears to play a crucial role in the insertion of secretory and membrane polypeptides into the endoplasmic reticulum. This protein found to be tightly associated with membrane-bound ribosomes, either directly or through adaptor proteins. This gene encodes an alpha subunit of the heteromeric SEC61 complex, which also contains beta and gamma subunits. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, SEC63, ACID, V1a, Ubiquitin
Papers on Sec61
Sec63 and Xbp1 regulate IRE1α activity and polycystic disease severity.
Lee et al., In J Clin Invest, May 2015
The HSP40 cochaperone SEC63 is associated with the SEC61 translocon complex in the ER.
Decatransin, a new natural product inhibiting protein translocation at the Sec61/SecYEG translocon.
Hoepfner et al., Basel, Switzerland. In J Cell Sci, Apr 2015
Chemogenomic profiling in S. cerevisiae indicated that the Sec61 translocon complex, the machinery for protein translocation and membrane insertion at the endoplasmic reticulum, is the target.
Proteasome 19S RP binding to the Sec61 channel plays a key role in ERAD.
Römisch et al., Saarbrücken, Germany. In Plos One, 2014
This indicates that the interaction between the 19S RP and the Sec61 channel is dependent on conformational changes in Sec61p hinging on loop 7. The sec61-S353C mutant had no measurable ER import defects and did not cause ER stress in intact cells, but reduced ER-export of a 19S RP-dependent misfolded protein when proteasomes were limiting in a cell-free assay.
Surveying the floodgates: estimating protein flux into the endoplasmic reticulum lumen in Saccharomyces cerevisiae.
Schnell et al., Ann Arbor, United States. In Front Physiol, 2013
In Saccharomyces cerevisiae the heterotrimeric endoplasmic reticulum translocon is composed of the Sec61p, Sss1p, and Sbh1p core subunits.
Cross-presentation of synthetic long peptides by human dendritic cells: a process dependent on ERAD component p97/VCP but Not sec61 and/or Derlin-1.
Guilloux et al., Nantes, France. In Plos One, 2013
Our data support a role for the ER-associated degradation machinery (ERAD)-related protein p97/VCP in the transport of SLP16-40 from early endosomes to the cytoplasm but formally exclude both sec61 and Derlin-1 as possible retro-translocation channels for cross-presentation.
Characterization of binding of LARP6 to the 5' stem-loop of collagen mRNAs: implications for synthesis of type I collagen.
Stefanovic et al., Tallahassee, United States. In Rna Biol, 2013
Loop 3 is also involved in the interaction of LARP6 and protein translocation channel SEC61.
BiP-mediated closing of the Sec61 channel limits Ca2+ leakage from the ER.
Zimmermann et al., Homburg, Germany. In Embo J, 2012
BiP limits ER Ca(2+) leakage through the Sec61 complex by binding to the ER lumenal loop 7 of Sec61alpha in the vicinity of tyrosine 344.
Tail-anchored membrane protein insertion into the endoplasmic reticulum.
Keenan et al., Cambridge, United Kingdom. In Nat Rev Mol Cell Biol, 2011
The well-studied co-translational pathway uses signal recognition particle (SRP) and its receptor for targeting and the SEC61 translocon for membrane integration.
Contribution of Sec61α to the life cycle of Ebola virus.
Kawaoka et al., Tokyo, Japan. In J Infect Dis, 2011
The present study indicates that Sec61alpha is a host protein involved in Ebola virus (EBOV) replication, specifically in EBOV genome transcription and replication.
Calmodulin regulation of the calcium-leak channel Sec61 is unique to vertebrates.
Jung et al., Osnabrück, Germany. In Channels (austin), 2011
CaM binding to the cytosolic N-terminus of Sec61alpha is involved in limiting Ca(2+)-leakage from the ER in C. familiaris but not S. cerevisiae.
Stability and function of the Sec61 translocation complex depends on the Sss1p tail-anchor sequence.
Andrews et al., Hamilton, Canada. In Biochem J, 2011
Sec61 post-translational translocation is dependent on assembly with Sss1p complexes.
Sec61 complexes form ubiquitous ER Ca2+ leak channels.
Zimmermann et al., Homburg, Germany. In Channels (austin), 2011
Silencing the SEC61A1 gene using two different siRNAs in HeLa cells for 96 hours had little effect on cell growth and viability. However, calcium leakage from the ER was greatly decreased in the SEC61A1-silenced cells.
Lysosomal proteolysis and autophagy require presenilin 1 and are disrupted by Alzheimer-related PS1 mutations.
Nixon et al., United States. In Cell, 2010
N-glycosylation of the V0a1 subunit, essential for its efficient ER-to-lysosome delivery, requires the selective binding of PS1 holoprotein to the unglycosylated subunit and the Sec61alpha/oligosaccharyltransferase complex.
Influence of protein-protein interactions on the cellular localization of cytochrome P450.
Kemper et al., Urbana, United States. In Expert Opin Drug Metab Toxicol, 2008
RESULTS/CONCLUSION: Targeting of CYPs to the ER is well understood and involves signal recognition particle-mediated delivery to the sec61 complex.
Real-time fluorescence detection of ERAD substrate retrotranslocation in a mammalian in vitro system.
Johnson et al., College Station, United States. In Cell, 2007
Retrotranslocation was blocked by antibodies against a putative retrotranslocation channel protein, derlin-1, but not Sec61alpha.
Endoplasmic reticulum-associated degradation.
Römisch, Cambridge, United Kingdom. In Annu Rev Cell Dev Biol, 2004
Secretory and transmembrane proteins enter the secretory pathway through the protein-conducting Sec61 channel in the membrane of the endoplasmic reticulum.
Cytotoxic ribosome-inactivating lectins from plants.
Lord et al., Coventry, United Kingdom. In Biochim Biophys Acta, 2004
Cell entry by ricin involves the following steps: (i) binding to cell-surface glycolipids and glycoproteins bearing beta-1,4-linked galactose residues through the lectin activity of the B-chain (RTB); (ii) uptake by endocytosis and entry into early endosomes; (iii) transfer by vesicular transport to the trans-Golgi network; (iv) retrograde vesicular transport through the Golgi complex and into the endoplasmic reticulum (ER); (v) reduction of the disulfide bond connecting the A- and B-chains; (vi) a partial unfolding of the A-chain (RTA) to enable it to translocate across the ER membrane via the Sec61p translocon using the pathway normally followed by misfolded ER proteins for targeting to the ER-associated degradation (ERAD) machinery; (vi) refolding in the cytosol into a protease-resistant, enzymatically active structure; (vii) interaction with the sarcin-ricin domain (SRD) of the large ribosome subunit RNA followed by cleavage of a single N-glycosidic bond in the RNA to generate a depurinated, inactive ribosome.
Ricin. Mechanisms of cytotoxicity.
Roberts et al., Coventry, United Kingdom. In Toxicol Rev, 2002
Cell entry by ricin involves a series of steps: (i) binding, via the ricin B chain (RTB), to a range of cell surface glycolipids or glycoproteins having beta-1,4-linked galactose residues; (ii) uptake into the cell by endocytosis; (iii) entry of the toxin into early endosomes; (iv) transfer, by vesicular transport, of ricin from early endosomes to the trans-Golgi network; (v) retrograde vesicular transport through the Golgi complex to reach the endoplasmic reticulum; (vi) reduction of the disulphide bond connecting the ricin A chain (RTA) and the RTB; (vii) partial unfolding of the RTA to render it translocationally-competent to cross the endoplasmic reticulum (ER) membrane via the Sec61p translocon in a manner similar to that followed by misfolded ER proteins that, once recognised, are targeted to the ER-associated protein degradation (ERAD) machinery; (viii) avoiding, at least in part, ubiquitination that would lead to rapid degradation by cytosolic proteasomes immediately after membrane translocation when it is still partially unfolded; (ix) refolding into its protease-resistant, biologically active conformation; and (x) interaction with the ribosome to catalyse the depurination reaction.
The Sec61p complex mediates the integration of a membrane protein by allowing lipid partitioning of the transmembrane domain.
Rapoport et al., Boston, United States. In Cell, 2000
We demonstrate that the Sec61p channel allows the TM domain to bypass the barrier posed by the polar head groups of the lipid bilayer and come into contact with the hydrophobic interior of the membrane.
Export of antigenic peptides from the endoplasmic reticulum intersects with retrograde protein translocation through the Sec61p channel.
Momburg et al., Heidelberg, Germany. In Immunity, 2000
Here we provide evidence that peptide export utilizes the Sec61p translocon as demonstrated by blocking this channel with bacterial exotoxin.
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