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Published August 2016 | public
Journal Article

Toward a structural understanding of co-translational protein translocation

Abstract

The translocation of most eukaryotic secreted and integral membrane proteins occurs co-translationally at the endoplasmic reticulum (ER). These nascent polypeptides are recognized on the ribosome by the signal recognition particle (SRP), targeted to the ER, and translocated across or inserted into the membrane by the Sec61 translocation channel. Structural analysis of these co-translational processes has been challenging due to the size, complexity, and flexibility of the targeting and translocation machinery. Recent technological advances in cryo-electron microscopy (cryo-EM) have resulted in increasingly powerful tools to study large, heterogeneous, and low-abundance samples. These advances are being utilized to obtain near-atomic resolution reconstructions of functional translation, targeting, and translocation intermediates, paving the way to a mechanistic understanding of protein biogenesis.

Additional Information

© 2016 Elsevier Ltd. Available online 6th May 2016. This work was supported by the UK Medical Research Council (MC_UP_A022_1007 to RSH) and a Wellcome Trust postdoctoral fellowship (R.M.V.).

Additional details

Created:
August 20, 2023
Modified:
October 18, 2023