Abstract：
:Dendritic cells (DCs) are the professional antigen-presenting cells (APC) which efficiently prime the immune response or induce tolerance. We recently identified Dendritic Cell Specific TrAnsMembrane Protein (DC-STAMP), a novel 470 amino acid protein preferentially expressed by dendritic cells. Previously we demonstrated that DC-STAMP re-localizes towards the Golgi upon DC maturation. To identify proteins that interact with DC-STAMP, a yeast-2-hybrid analysis was performed. Here, we report a physically interacting partner of DC-STAMP in the endoplasmic reticulum (ER), called LUMAN (also known as CREB3 or LZIP). LUMAN was previously described as an ER-resident transcription factor with unknown function. It is activated in a process called regulated intramembrane proteolysis (RIP), which involves translocation to the Golgi and subsequent proteolytic cleavage. The proteolytically activated form of the protein then translocates to the nucleus. Our data indicate that DC-STAMP plays an important role in the modulation of LUMAN activation. Moreover, we demonstrate that LUMAN is endogenously expressed by DC and becomes activated by RIP upon DC maturation induced by various different stimuli. These data define LUMAN/DC-STAMP as a novel regulatory circuit in DC.
journal_name
Mol Immunoljournal_title
Molecular immunologyauthors
Eleveld-Trancikova D,Sanecka A,van Hout-Kuijer MA,Looman MW,Hendriks IA,Jansen BJ,Adema GJdoi
10.1016/j.molimm.2010.04.019subject
Has Abstractpub_date
2010-07-01 00:00:00pages
1963-73issue
11-12eissn
0161-5890issn
1872-9142pii
S0161-5890(10)00158-6journal_volume
47pub_type
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