CREB3L3 translocates from the endoplasmic reticulum membrane to the Golgi membrane

Stable Identifier
Reaction [omitted]
Homo sapiens
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Unlike ATF6, CREB3L3 (and probably other CREB3 family members) does not interact with HSPA5 (BiP) (Llarena 2010). Instead, retention in the endoplasmic reticulum (ER) is mediated by a membrane-proximal cytoplasmic motif (Bailey et al. 2007). When the motif is deleted CREB3L3 is constitutively trafficked to the Golgi where it is cleaved (Bailey et al. 2007). In cells not experiencing ER stress, CREB3L3 is located in the ER membrane (Stirling and O'Hare 2006, Bailey et al. 2007, Llarena et al. 2010) and is rapidly turned over by the endoplasmic reticulum associated degradation (ERAD) pathway (Bailey et al. 2007). During ER stress CREB3L3 is translocated by an uncharacterized mechanism to the Golgi (Bailey et al. 2007, Llarena et al. 2010, also inferred from the mouse homolog in Zhang et al. 2006). CREB3L3 is expressed strongly in the liver and more weakly in the stomach and small intestine.
Literature References
PubMed ID Title Journal Year
16469704 Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response

Kaufman, RJ, Zhang, K, Back, SH, Shen, X, Sakaki, K, Wu, J, Rutkowski, DT, Saunders, T

Cell 2006
19883396 Different mechanisms of recognition and ER retention by transmembrane transcription factors CREB-H and ATF6

O'Hare, P, Bailey, D, Curtis, H, Llarena, M

Traffic 2010
17875199 Trafficking of the bZIP transmembrane transcription factor CREB-H into alternate pathways of ERAD and stress-regulated intramembrane proteolysis

O'Hare, P, Bailey, D, Barreca, C

Traffic 2007
16236796 CREB4, a transmembrane bZip transcription factor and potential new substrate for regulation and cleavage by S1P

O'Hare, P, Stirling, J

Mol. Biol. Cell 2006
Orthologous Events
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