High impact information on Nfkb1

• Nuclear Akt associates with PKC-phosphorylated Ebp1, preventing DNA fragmentation by inhibition of caspase-activated DNase [1].
• Thus, nuclear Akt might contribute to suppressing apoptosis through interaction with Ebp1 [1].
• Ebp1 (S360A), which cannot be phosphorylated by PKC, barely binds Akt or inhibits DNA fragmentation, whereas Ebp1 S360D, which mimics phosphorylation, strongly binds Akt and suppresses apoptosis [1].
• Depletion of Ebp1 from nuclear extracts or knockdown of Ebp1 in PC12 cells abolishes the protective effects of nerve growth factor, whereas overexpression of Ebp1 prevents apoptosis [1].
• Thus, Ebp1 might regulate cell survival and differentiation through two distinctive p48 and p42 isoforms [2].

Biological context of Nfkb1

• This proposed signaling pathway does not require the continuous upregulation of Nfkb1 or the other assayed transcription factors as early as 12 h after middle ear infection [3].
• Ebp1 binds nuclear Akt and prevents DNA fragmentation by inhibiting caspase-activated DNase [2].
• Ebp1 isoforms distinctively regulate cell survival and differentiation [2].
• EGF strongly stimulates p42 to bind ErbB3, and the association depends on PKC-mediated phosphorylation of Ebp1 [2].

Anatomical context of Nfkb1

• Here, we show that Ebp1 possesses two different isoforms, p48 and p42, which differentially mediate PC12 cell survival and differentiation [2].

Other interactions of Nfkb1

• The altered expression of those genes in MEM was validated and quantified using real-time polymerase chain reaction and MEM protein expression for Atp1a1, Nos2 and Nfkb1 was studied using Western blot and/or immunohistochemistry assays [3].

References