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in vivo bioluminescence imaging in a transgenic model of inflammation showed that luciferase activity coincided with endogenous p52/p100 Nfkb2 expression
our studies for the first time establish p100 (zeige PATL2 Proteine) as a key tumor suppressor of bladder cancer growth
hyperresponsive promoter engaged the RelA:p52 dimer generated during costimulation of macrophages through TLR4 (zeige TLR4 Proteine) and LTbetaR to trigger synthesis of IkappaBalpha (zeige NFKBIA Proteine) at late time points, which prevented the late-acting RelA (zeige NFkBP65 Proteine) cross-talk response.
results suggest that changes in the relative concentrations of RelB (zeige RELB Proteine), NIK:IKK1, and p100 (zeige PATL2 Proteine) during noncanonical signaling modulate this transitional complex and are critical for maintaining the fine balance between the processing and protection of p100 (zeige PATL2 Proteine).
Results suggest that the RelB (zeige RELB Proteine)/NF-kappaB2 pathway regulates T cell migration to autoimmune targets in Sjogren syndrome through TGFbeta (zeige TGFB1 Proteine)/TGFbetaR-dependent regulation of CXCL12 (zeige CXCL12 Proteine)/CXCR4 (zeige CXCR4 Proteine) signaling.
MKK4 (zeige MAP2K4 Proteine) activates non-canonical NFkappaB signaling by promoting NFkappaB2-p100 (zeige PATL2 Proteine) processing.
the aberrant proliferative capacity of Brca1 (zeige BRCA1 Proteine)(-/-) luminal progenitor cells is linked to the replication-associated DNA damage response, where proliferation of mammary progenitors is perpetuated by damage-induced, autologous NF-kappaB (zeige NFKB1 Proteine) signaling.
RelB (zeige RELB Proteine) is processed by CO2 in a manner dependent on a key C-terminal domain located in its transactivation domain. Loss of the RelB (zeige RELB Proteine) transactivation domain alters NF-kappaB (zeige NFKB1 Proteine)-dependent transcriptional activity, and loss of p100 (zeige PATL2 Proteine) alters sensitivity of RelB (zeige RELB Proteine) to CO2
the individual functions of the NF-kappaB (zeige NFKB1 Proteine) family members NF-kappaB1 (zeige NFKB1 Proteine), NF-kappaB2 and c-REL (zeige NFkBP65 Proteine) in the various autoimmune pathologies of Fas(lpr/lpr (zeige FAS Proteine)) mutant mice, were investigated.
we identify in this study a critical role for the combined activity of the RELB (zeige RELB Proteine) and NF-kappaB2 subunits in B cell homeostasis that cannot be compensated for by the canonical NF-kappaB (zeige NFKB1 Proteine) pathway under physiological conditions.
NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF- kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF- kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. In a non-canonical activation pathway, the MAP3K14- activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes. The NF-kappa-B heterodimeric RelB-p52 complex is a transcriptional activator. The NF-kappa-B p52-p52 homodimer is a transcriptional repressor. NFKB2 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p100 and generation of p52 by a cotranslational processing. The proteasome-mediated process ensures the production of both p52 and p100 and preserves their independent function. p52 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. p52 and p100 are respectively the minor and major form\; the processing of p100 being relatively poor. Isoform p49 is a subunit of the NF-kappa-B protein complex, which stimulates the HIV enhancer in synergy with p65 (By similarity).
DNA-binding factor KBF2
, NF kappaB2
, nuclear factor NF-kappa-B p100 subunit
, nuclear factor of kappa light polypeptide gene enhancer in B-cells 2, p49/p100