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Protein targeting and translocation at the endoplasmic reticulum membrane--through the eye of a needle?

Authors
  • Meacock, S L
  • Greenfield, J J
  • High, S
Type
Published Article
Journal
Essays in biochemistry
Publication Date
Jan 01, 2000
Volume
36
Pages
1–13
Identifiers
PMID: 12471898
Source
Medline
License
Unknown

Abstract

SRP-dependent and SRP-independent targeting routes deliver precursor proteins to the ER membrane translocon. These precursors are translocated into (for membrane proteins) and across (for secretory protein) the ER membrane via aqueous channels composed of oligomers of the Sec61 complex. Both ends of the ER translocon are 'gated' and the opening and closing of these gates are closely regulated. The lateral exit of hydrophobic polypeptide regions into the phospholipid bilayer also appears to be a carefully controlled process. Accessory components are transiently associated with active ER translocation sites and modify the nascent polypeptide as it appears on the luminal side of the membrane.

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