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Published January 27, 2017 | Accepted Version + Supplemental Material
Journal Article Open

An N-end rule pathway that recognizes proline and destroys gluconeogenic enzymes


Cells synthesize glucose if deprived of it, and destroy gluconeogenic enzymes upon return to glucose-replete conditions. We found that the Gid4 subunit of the ubiquitin ligase GID in the yeast Saccharomyces cerevisiae targeted the gluconeogenic enzymes Fbp1, Icl1, and Mdh2 for degradation. Gid4 recognized the N-terminal proline (Pro) residue and the ~5-residue-long adjacent sequence motifs. Pck1, the fourth gluconeogenic enzyme, contains Pro at position 2; Gid4 directly or indirectly recognized Pro at position 2 of Pck1, contributing to its targeting. These and related results identified Gid4 as the recognition component of the GID-based proteolytic system termed the Pro/N-end rule pathway. Substrates of this pathway include gluconeogenic enzymes that bear either the N-terminal Pro residue or a Pro at position 2, together with adjacent sequence motifs.

Additional Information

© 2017 American Association for the Advancement of Science. Received 8 November 2016; accepted 14 December 2016. We thank P. Bjorkman (Caltech) for her comments on the manuscript, and A. Melnykov and other members of the Varshavsky laboratory for discussions and helpful suggestions. Supported by NIH grants DK039520 and GM031530 (A.V.).

Attached Files

Accepted Version - nihms859347.pdf

Supplemental Material - Chen.SM.pdf


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