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Title 

Yeast SREBP cleavage activation requires the golgi Dsc E3 ligase complex

Authors 

E V StewartC C NwosuZ TongA RoguevT D CumminsDong Uk KimJ HaylesH O ParkKwang Lae HoeD W PowellN J KroganP J Espenshade

Publisher 

Elsevier (Cell Press)

Issue Date 

2011

Citation 

Molecular Cell, vol. 42, no. 2, pp. 160-171

Abstract 

Mammalian lipid homeostasis requires proteolytic activation of membrane-bound sterol regulatory element binding protein (SREBP) transcription factors through sequential action of the Golgi Site-1 and Site-2 proteases. Here we report that while SREBP function is conserved in fungi, fission yeast employs a different mechanism for SREBP cleavage. Using genetics and biochemistry, we identified four genes defective for SREBP cleavage, dsc1-4, encoding components of a transmembrane Golgi E3 ligase complex with structural homology to the Hrd1 E3 ligase complex involved in endoplasmic reticulum-associated degradation. The Dsc complex binds SREBP and cleavage requires components of the ubiquitin-proteasome pathway: the E2-conjugating enzyme Ubc4, the Dsc1 RING E3 ligase, and the proteasome. dsc mutants display conserved aggravating genetic interactions with components of the multivesicular body pathway in fission yeast and budding yeast, which lacks SREBP. Together, these data suggest that the Golgi Dsc E3 ligase complex functions in a post-ER pathway for protein degradation.

ISSN 

1097-2765

Link 

http://dx.doi.org/10.1016/j.molcel.2011.02.035

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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