Electronic Resource
Palo Alto, Calif.
:
Annual Reviews
Annual Review of Cell and Developmental Biology
21 (2005), S. 435-456
ISSN:
1081-0706
Source:
Annual Reviews Electronic Back Volume Collection 1932-2001ff
Topics:
Biology
,
Medicine
Notes:
Secretory and transmembrane proteins enter the secretory pathway through the protein-conducting Sec61 channel in the membrane of the endoplasmic reticulum. In the endoplasmic reticulum, proteins fold, are frequently covalently modified, and oligomerize before they are packaged into transport vesicles that shuttle them to the Golgi complex. Proteins that misfold in the endoplasmic reticulum are selectively transported back across the endoplasmic reticulum membrane to the cytosol for degradation by proteasomes. Depending on the topology of the defect in the protein, cytosolic or lumenal chaperones are involved in its targeting to degradation. The export channel for misfolded proteins is likely also formed by Sec61p. Export may be powered by AAA-ATPases of the proteasome 19S regulatory particle or Cdc48p/p97. Exported proteins are frequently ubiquitylated prior to degradation and are escorted to the proteasome by polyubiquitin-binding proteins.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1146/annurev.cellbio.21.012704.133250
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