Editors' ChoiceCell Biology

Trashing Misfolded Membrane Proteins

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Science Signaling  11 Nov 2014:
Vol. 7, Issue 351, pp. ec317
DOI: 10.1126/scisignal.aaa2495

Proteins move to and from the inner nuclear membrane from the rest of the endoplasmic reticulum through the nuclear pores. This movement is tightly controlled. Consequently, the inner nuclear membrane accumulates a specific set of proteins required for various functions, including chromosome organization and transcriptional control. But when inner nuclear membrane proteins misfold, how are they eliminated? Foresti et al. addressed this question in yeast and found that a previously elusive branch of the endoplasmic reticulum–associated degradation system was key (see the Perspective by Shao and Hegde).

O. Foresti, V. Rodriguez-Vaello, C. Funaya, P. Carvalho, Quality control of inner nuclear membrane proteins by the Asi complex. Science 346, 751–755 (2014). [Abstract] [Full Text]

S. Shao, R. S. Hegde, Local synthesis and disposal. Science 346, 701–7025 (2014). [Abstract] [Full Text]

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