Nuclear shuttling of yeast scaffold Ste5 is required for its recruitment to the plasma membrane and activation of the mating MAPK cascade
Article Abstract:
The localization of Ste5 to the plasma membrane's Gbeta region, essential for pheromone signal transmission to associated MAP kinase cascade enzymes, is shown to require the prior nuclear shuttling of Ste5. The study also reveal that Ste5 that are unable to transit the nucleus are not capable of settling at the periphery and activating the pathway. This regulatory mechanism may help ensure that cytoplasmic Ste5 do not activate downstream kinases and could be applicable to other signaling proteins.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1999
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The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites
Article Abstract:
The crystal structure of yeast protein disulfide isomerase reveals that the four thioredoxin domains are arranged in the shape of a twisted 'U' with the active sites facing each other across the long sides of the 'U'. The structure defines a framework for rationalizing the differences between the two active sites and their respective roles in catalyzing the formation and rearrangement of disulfide bonds.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2006
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