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Dynamics and retention of misfolded proteins in native ER membranes.

Abstract：

:When co-translationally inserted into endoplasmic reticulum (ER) membranes, newly synthesized proteins encounter the lumenal environment of the ER, which contains chaperone proteins that facilitate the folding reactions necessary for protein oligomerization, maturation and export from the ER. Here we show, using a temperature-sensitive variant of vesicular stomatitis virus G protein tagged with green fluorescent protein (VSVG-GFP), and fluorescence recovery after photobleaching (FRAP), the dynamics of association of folded and misfolded VSVG complexes with ER chaperones. We also investigate the potential mechanisms underlying protein retention in the ER. Misfolded VSVG-GFP complexes at 40 degrees C are highly mobile in ER membranes and do not reside in post-ER compartments, indicating that they are not retained in the ER by immobilization or retrieval mechanisms. These complexes are immobilized in ATP-depleted or tunicamycin-treated cells, in which VSVG-chaperone interactions are no longer dynamic. These results provide insight into the mechanisms of protein retention in the ER and the dynamics of protein-folding complexes in native ER membranes.

journal_name

Nat Cell Biol

journal_title

Nature cell biology

authors

Nehls S,Snapp EL,Cole NB,Zaal KJ,Kenworthy AK,Roberts TH,Ellenberg J,Presley JF,Siggia E,Lippincott-Schwartz J

doi

10.1038/35010558

keywords:

subject

Has Abstract

pub_date

2000-05-01 00:00:00

pages

288-95

issue

5

eissn

1465-7392

issn

1476-4679

journal_volume

2

pub_type

杂志文章

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