CREB3 translocates from the cytosol to the nucleus

Stable Identifier
Reaction [omitted]
Homo sapiens
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Based on homology with other substrates of regulated intramembrane cleavage, cleavage by regulate intramembrane proteolysis is believed to release the N-terminal cytoplasmic domain of CREB3 into the cytosol (Raggo et al. 2002, Eleveld-Trancikova et al. 2010). The fragment is then translocated into the nucleus (Raggo et al. 2002, Eleveld-Trancikova et al. 2010) where, in combination with HCF-1, it activates target genes that contain UPRE and ERSE-II elements in their promoters (Liang et al. 2006).

Literature References
PubMed ID Title Journal Year
20546900 DC-STAMP interacts with ER-resident transcription factor LUMAN which becomes activated during DC maturation

van Hout-Kuijer, MA, Eleveld-Trancikova, D, Jansen, BJ, Sanecka, A, Adema, GJ, Hendriks, IA, Looman, MW

Mol. Immunol. 2010
16940180 Luman/CREB3 induces transcription of the endoplasmic reticulum (ER) stress response protein Herp through an ER stress response element

Lu, R, Martyn, AC, Dean, JD, Cockram, GP, Kokame, K, Li, Y, Audas, TE, Liang, G

Mol. Cell. Biol. 2006
12138176 Luman, the cellular counterpart of herpes simplex virus VP16, is processed by regulated intramembrane proteolysis

O'Hare, P, Raggo, C, Gobeil, P, Misra, V, Smith-Windsor, E, Stirling, J, Rapin, N

Mol. Cell. Biol. 2002
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