Different degradation pathways for heterologous glycoproteins in yeast

FEBS Letters

Makarow, Marja¹  Holkeri, Heidi¹ 

[1] Institute of Biotechnology, Viikinkaari 9, 00710 Helsinki, Finland

关键词: Protein folding;    Protein degradation;    Chaperone;    Saccharomyces cerevisiae;   

DOI  :  10.1016/S0014-5793(98)00586-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Rat nerve growth factor receptor ectodomain (NGFR_e) and Escherichia coli β-lactamase were translocated into the yeast endoplasmic reticulum (ER), glycosylated, misfolded and rapidly degraded. NGFR_e underwent ATP-dependent thermosensitive degradation independently of vesicular transport. Since no evidence for degradation by the cytoplasmic 26S proteosome complex could be obtained, NGFR_e appeared to be degraded in the ER. β-Lactamase exited the ER by vesicular traffic and was transported from the Golgi via the Vps10 receptor pathway to the vacuole for degradation. Machineries in the ER and the Golgi appear to recognize distinct structural features on misfolded heterologous proteins and guide them to different degradation pathways.

【 授权许可】

Unknown