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- _3 value "NF-?B transcriptional activity can be also regulated independently of I? B degradation by the direct phosphorylation of NF-?B subunits. The phosphorylation of NF-?B was demonstrated with I?B kinases [47, 48], protein kinase CK2 (formerly casein kinase II) [49, 50], protein kinase A (PKA) [51], phosphatidylinositol 3-kinase (PI3K) [52, 53] and protein kinase C? (PKC?) [53, 54]. In addition, mitogen-activated protein (MAP) kinase regulated the activity of NF-? B independently of the NF-? B phosphorylation [55]. Summary: NFKB1 (MIM 164011 ) or NFKB2 (MIM 164012 ) is bound to REL (MIM 164910 ), RELA (MIM 164014 ), or RELB (MIM 604758 ) to form the NFKB complex. The NFKB complex is inhibited by I-kappa-B proteins (NFKBIA, MIM 164008 , or NFKBIB, MIM 604495 ), which inactivate NF-kappa-B by trapping it in the cytoplasm. Phosphorylation of serine residues on the I-kappa-B proteins by kinases (IKBKA, MIM 600664 , or IKBKB) marks them for destruction via the ubiquitination pathway, thereby allowing activation of the NF-kappa-B complex. Activated NFKB complex translocates into the nucleus and binds DNA at kappa-B-binding motifs such as 5-prime GGGRNNYYCC 3-prime or 5-prime HGGARNYYCC 3-prime (where H is A, C, or T; R is an A or G purine; and Y is a C or T pyrimidine).[supplied by OMIM] The induction of cell motility has been linked to the activation of PI 3-kinase [57], and a significant increase of PI-3 kinase activity was detected in highly invasive MDA-MB-231 cells over that observed in MCF-7 cells [58]. However, the motility of breast cancer cells MDA-MB-231 was suppressed by the overexpression of dominant negative regulatory (p85?) subunit, as well as by the inhibition of catalytic (p110) subunit by specific inhibitors of p110, wortmannin and LY294002 [58]." provenance.