ER-Associated Degradation of Membrane Proteins in Yeast | Zendy

Cédric Pety de Thozée | Zendy; Michel Ghislain | Zendy

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ER-Associated Degradation of Membrane Proteins in Yeast

Author(s) -

Cédric Pety de Thozée,

Michel Ghislain

Publication year - 2006

Publication title -

the scientific world journal

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.453

H-Index - 93

eISSN - 2356-6140

pISSN - 1537-744X

DOI - 10.1100/tsw.2006.191

Subject(s) - endoplasmic reticulum , copii , proteasome , microbiology and biotechnology , protein subunit , endoplasmic reticulum associated protein degradation , membrane protein , cytosol , secretory pathway , secretory protein , protein folding , protein degradation , transport protein , chemistry , biochemistry , biology , unfolded protein response , membrane , secretion , enzyme , golgi apparatus , gene

Proteins destined for the secretory pathway are translocated into the endoplasmic reticulum (ER), where they are subjected to a variety of post-translational modifications before they reach their final destination. Newly synthesized proteins that have defect in polypeptide folding or subunit assembly are recognized by quality control systems and eliminated by the 26S proteasome, a cytosolic ATP-dependent proteolytic machinery. Delivery of non-native ER proteins to the proteasome requires retrograde transport across the ER membrane and depends on a protein-unfolding machine consisting of Cdc48p, Ufd1p, and Npl4p. Recent studies in yeast have highlighted the possible function of the Sar1p/COPII machinery in ER-associated degradation of some lumenal and membrane proteins.

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