MBTPS2 (S2P) cleaves CREB3

Stable Identifier
R-HSA-8874192
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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CREB3 is cleaved by regulated intramembrane proteolysis (RIP) (Raggo et al. 2002, Liang et al. 2006, Eleveld-Trancikova et al. 2010). As inferred from other RIP susbsrates, MBTPS2 (S2P) is believed to cleave CREB3 after MBTPS1 (S1P) cleaves (Raggo et al. 2002). Based on homology with cleavage sites in SREBP (SREBF) homologues, the cleavage site in CREB3 is estimated to be at about amino acid 254 at the cytoplasmic face of the transmembrane domain (Raggo et al. 2002).

Literature References
PubMed ID Title Journal Year
16940180 Luman/CREB3 induces transcription of the endoplasmic reticulum (ER) stress response protein Herp through an ER stress response element

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

Mol. Cell. Biol. 2006
20546900 DC-STAMP interacts with ER-resident transcription factor LUMAN which becomes activated during DC maturation

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

Mol. Immunol. 2010
12138176 Luman, the cellular counterpart of herpes simplex virus VP16, is processed by regulated intramembrane proteolysis

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

Mol. Cell. Biol. 2002
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
metalloendopeptidase activity of MBTPS2 [Golgi membrane]
Physical Entity
Activity
Inferred From
Authored
Reviewed
Created