Dataset Information


Hrd1 interaction proteomics - Lipid disequilibrium disrupts ER proteostasis by impairing ERAD substrate glycan trimming and dislocation

ABSTRACT: Endoplasmic reticulum (ER)-associated degradation (ERAD) mediates the degradation of misfolded and unoligomerized proteins in the early secretory pathway. ERAD substrates are detected and delivered to membrane-embedded dislocation complexes. Following transfer into the cytosol, substrates are rapidly ubiquitinated and targeted to the 26S proteasome for degradation. Hrd1 is a highly conserved, ER-resident E3 ubiquitin-protein ligase that functions in ERAD. In this study, we employed stable isotope labeling with amino acids in cell culture (SILAC) to quantitatively assess the impact of altered lipid homeostasis on the composition of S-tagged Hrd1 complexes affinity purified from HEK293 cells. Although lipid disequilibrium impaired ERAD substrate delivery to Hrd1, the overall composition of the Hrd1 complex was unaffected.

INSTRUMENT(S): 6410 Triple Quadrupole LC/MS

ORGANISM(S): Homo sapiens  

TISSUE(S): Cell Culture

DISEASE(S): Not Available

SUBMITTER: James Olzmann  

LAB HEAD: James Arthur Olzmann

PROVIDER: PXD005633 | Pride | 2017-01-03


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Lipid disequilibrium disrupts ER proteostasis by impairing ERAD substrate glycan trimming and dislocation.

To Milton M   Peterson Clark W H CW   Roberts Melissa A MA   Counihan Jessica L JL   Wu Tiffany T TT   Forster Mercedes S MS   Nomura Daniel K DK   Olzmann James A JA  

Molecular biology of the cell 20161123 2

The endoplasmic reticulum (ER) mediates the folding, maturation, and deployment of the secretory proteome. Proteins that fail to achieve their native conformation are retained in the ER and targeted for clearance by ER-associated degradation (ERAD), a sophisticated process that mediates the ubiquitin-dependent delivery of substrates to the 26S proteasome for proteolysis. Recent findings indicate that inhibition of long-chain acyl-CoA synthetases with triacsin C, a fatty acid analogue, impairs li  ...[more]

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