Mammalian Sec61 is associated with Sec62 and Sec63 (Q22254037)

signaling receptor activity

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

H A Meyer

1

H A

Meyer

1 reference

8 February 2023

H Grau

2

H

Grau

1 reference

8 February 2023

R Kraft

3

R

Kraft

1 reference

8 February 2023

S Kostka

4

S

Kostka

1 reference

8 February 2023

S Prehn

5

S

Prehn

1 reference

8 February 2023

K U Kalies

6

K U

Kalies

1 reference

8 February 2023

E Hartmann

7

E

Journal of Biological Chemistry

Hartmann

1 reference

8 February 2023

language of work or name

English

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publication date

12 May 2000

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published in

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volume

275

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issue

19

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page(s)

14550-7

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cites work

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A protein-conducting channel in the endoplasmic reticulum.

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Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane

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Oligomeric Rings of the Sec61p Complex Induced by Ligands Required for Protein Translocation

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Alignment of conduits for the nascent polypeptide chain in the ribosome-Sec61 complex

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Binding of ribosomes to the rough endoplasmic reticulum mediated by the Sec61p-complex

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Signal sequence recognition in cotranslational translocation by protein components of the endoplasmic reticulum membrane

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A protein of the endoplasmic reticulum involved early in polypeptide translocation

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Purification of microsomal signal peptidase as a complex

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Signal peptide fragments of preprolactin and HIV-1 p-gp160 interact with calmodulin

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The beta subunit of the Sec61 complex facilitates cotranslational protein transport and interacts with the signal peptidase during translocation

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Oligosaccharyltransferase activity is associated with a protein complex composed of ribophorins I and II and a 48 kd protein

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A signal sequence receptor in the endoplasmic reticulum membrane

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Control of glycosylation of MHC class II-associated invariant chain by translocon-associated RAMP4.

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Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle

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Lumenal proteins of the mammalian endoplasmic reticulum are required to complete protein translocation.

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A yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulum

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Evolutionary conservation of components of the protein translocation complex

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Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex

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Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p

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Topology and functional domains of Sec63p, an endoplasmic reticulum membrane protein required for secretory protein translocation

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BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane

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Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast

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Nonlethal sec71-1 and sec72-1 mutations eliminate proteins associated with the Sec63p-BiP complex from S. cerevisiae

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KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene

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ER membrane protein complex required for nuclear fusion

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Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation

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Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation

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A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation

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Structure and biosynthesis of the signal-sequence receptor.

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A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s

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Identification of a human cDNA homologue to the Drosophila translocation protein 1 (Dtrp1)

21 January 2018

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M13 procoat and a pre-immunoglobulin share processing specificity but use different membrane receptor mechanisms

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Ribonucleoparticle-independent import of proteins into mammalian microsomes involves a membrane protein which is sensitive to chemical alkylation.

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The membrane proteins TRAMp and sec61 alpha p may be involved in post-translational transport of presecretory proteins into mammalian microsomes.

21 January 2018

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New variation on the translocation of proteins during early biogenesis of apolipoprotein B.

21 January 2018

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A microsomal ATP-binding protein involved in efficient protein transport into the mammalian endoplasmic reticulum.

21 January 2018

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7 January 2021

A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane

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7 January 2021

BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation

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7 January 2021

The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct

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https://api.crossref.org/works/10.1074%2FJBC.275.19.14550

7 January 2021