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MBC in Press, published online ahead of print October 19, 2005
Mol. Biol. Cell 10.1091/mbc.E05-06-0500

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Submitted on June 8, 2005
Revised on August 30, 2005
Accepted on October 7, 2005

CREB4, a Transmembrane bZip Transcription Factor and Potential New Substrate for Regulation and Cleavage by S1P

Julie Stirling and Peter O’Hare

Marie Curie Research Institute, Oxted RH8 0TL, United Kingdom

Monitoring Editor: Jennifer Lippincott-Schwartz

Regulated intramembrane proteolysis of the factors SREBP and ATF6, represents a central control mechanism in sterol homeostasis and stress response within the endoplasmic reticulum. Here we compare localization of ATF6-related bZip factors, CREB4, CREB-H, Luman and OASIS. These factors contain the defining features of a bZip domain, a predicted transmembrane domain and an adjacent cleavage site for the Golgi protease S1P, with conserved features which indicate that it represents a specific subclass of S1P sites. Each factor localizes to the ER, while a population of CREB4 was also observed in the Golgi. Deletion of the transmembrane domain in CREB4, resulted in efficient nuclear accumulation. An N-terminal variant of CREB4 containing the BZIp domain potently activated expression from a target gene containing ATF6 binding sites and from the promoter for the ER chaperone GRP78/BIP. CREB4 was cleaved in a site specific manner in response to Brefeldin A disruption of the Golgi or by coexpression with S1P but only after deletion or substitution of its C-terminal lumenal domain. Thus S1P cleavage of CREB4 may be suppressed by a determinant in the C-terminal region. Dithiothreitol induced more complete transport of CREB4 to the Golgi, but not cleavage. Together the data identify at least one additional bZip factor whose localization responds to ER stress and we propose a model based on these results which indicate additional levels of control of this novel class of transcription factors.

Address correspondence to: Peter O’Hare (p.ohare{at}mcri.ac.uk)




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