Proteomics

Dataset Information

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Substrates of human TRAP complex


ABSTRACT: While the Sec61-complex in the membrane of the human endoplasmic reticulum facilitates translocation of all precursor polypeptides with amino-terminal signal peptides or transmembrane helices, the Sec61-associated translocon-associated protein (TRAP)-complex supports translocation of only a subset of precursor polypeptides, i.e. in a substrate-specific manner. To characterize TRAP-dependent precursors, we combined siRNA-mediated TRAP depletion in HeLa cells, label-free quantitative proteomics, and differential expression analysis. Sec61 served as a positive control

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Nagarjuna Nagaraj  

LAB HEAD: Prof. Dr. Richard Zimmermann

PROVIDER: PXD008178 | Pride | 2018-08-09

REPOSITORIES: Pride

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Publications

Proteomics reveals signal peptide features determining the client specificity in human TRAP-dependent ER protein import.

Nguyen Duy D   Stutz Regine R   Schorr Stefan S   Lang Sven S   Pfeffer Stefan S   Freeze Hudson H HH   Förster Friedrich F   Helms Volkhard V   Dudek Johanna J   Zimmermann Richard R  

Nature communications 20180914 1


In mammalian cells, one-third of all polypeptides are transported into or across the ER membrane via the Sec61 channel. While the Sec61 complex facilitates translocation of all polypeptides with amino-terminal signal peptides (SP) or transmembrane helices, the Sec61-auxiliary translocon-associated protein (TRAP) complex supports translocation of only a subset of precursors. To characterize determinants of TRAP substrate specificity, we here systematically identify TRAP-dependent precursors by an  ...[more]

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