Journal
BIOCHEMICAL JOURNAL
Volume 456, Issue -, Pages 297-309Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BJ20130100
Keywords
endoplasmic reticulum; membrane protein folding; potassium channel protein of chlorella virus (Kcv channel); site-specific cross-linking; TWIK (tandem-pore weak inwardly rectifying potassium channel)-related acid-sensitive potassium channel 1 (TASK-1)
Categories
Funding
- Wellcome Trust [093176/Z/10/A]
- [088163/Z/09/Z]
- Wellcome Trust [093176/Z/10/A] Funding Source: Wellcome Trust
Ask authors/readers for more resources
The majority of the polytopic proteins that are synthesized at the ER (endoplasrnic reticulum) are integrated co-translationally via the Sec61 translocon, which provides lateral access for their hydrophobic TMs (transmembrane regions) to the phospholipid bilayer. A prolonged association between TMs of the potassium channel subunit, TASK-1 [TWIK (tandem-pore weak inwardly rectifying potassium channel)-related acid-sensitive potassium channel 1], and the Sec61 complex suggests that the ER translocon co-ordinates the folding/assembly of the TMs present in the nascent chain. The N-terminus of both TASK-1 and Kcv (potassium channel protein of chlorella virus), another potassium channel subunit of viral origin, has access to the N-glycosylation machinery located in the ER lumen, indicating that the Sec61 complex can accommodate multiple arrangements/orientations of TMs within the nascent chain, both in vitro and in vivo. Hence the ER translocon can provide the ribosome-bound nascent chain with a dynamic environment in which it can explore a range of different conformations en route to its correct transmembrane topology and final native structure.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available