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EDEM1 interaction proteomics in HEK293T cells

ABSTRACT: Misfolded or unfolded proteins from the endoplasmic reticulum (ER) are sent to proteasomal degradation via the Endoplasmic Reticulum Associated Degradation (ERAD) pathway. We provide here a proteomic analysis of the interaction partners for one of the ER mannosidases involved in ERAD, ER degradation-enhancing alpha-mannosidase-like protein 1 (EDEM1) and its mutant, a previously described version of EDEM, lacking its N-terminal disordered region (Δ-EDEM1). Moreover, we also performed a whole proteome analysis for cells overexpressing both, WT and Δ-EDEM1 and investigated the proteins which co-fractionate in a sucrose gradient for both EDEM1 and Δ-EDEM1 and their associated proteins.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Cristian Munteanu

LAB HEAD: Ștefana M. Petrescu

PROVIDER: PXD019066 | Pride | 2020-05-20

REPOSITORIES: Pride

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EDEM1 Drives Misfolded Protein Degradation via ERAD and Exploits ER-Phagy as Back-Up Mechanism When ERAD Is Impaired.

Chiritoiu Marioara M Chiritoiu Gabriela N GN Munteanu Cristian V A CVA Pastrama Florin F Ivessa N Erwin NE Petrescu Stefana M SM

International journal of molecular sciences 20200514 10

Endoplasmic reticulum (ER)-associated degradation (ERAD) is the main mechanism of targeting ER proteins for degradation to maintain homeostasis, and perturbations of ERAD lead to pathological conditions. ER-degradation enhancing α-mannosidase-like (EDEM1) was proposed to extract terminally misfolded proteins from the calnexin folding cycle and target them for degradation by ERAD. Here, using mass-spectrometry and biochemical methods, we show that EDEM1 is found in auto-regulatory complexes with ...[more]

PMID: 32423001

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