General (macro)autophagy and the activation of NFκB constitute prominent 
responses to a large array of intracellular and extracellular stress conditions. 
The depletion of any of the three subunits of the inhibitor of NFκB (IκB) kinase 
(IKKα, IKKβ, IKKγ/NEMO), each of which is essential for the canonical NFκB 
activation pathway, limits autophagy induction by physiological or 
pharmacological triggers, while constitutive active IKK subunits suffice to 
stimulate autophagy. The activation of IKK usually relies on TGFβ-activated 
kinase 1 (TAK1), which is also necessary for the optimal induction of autophagy 
in multiple settings. TAK1 interacts with two structurally similar 
co-activators, TAK1-binding proteins 2 and 3 (TAB2 and TAB3). Importantly, in 
resting conditions both TAB2 and TAB3 bind the essential autophagic factor 
Beclin 1, but not TAK1. In response to pro-autophagic stimuli, TAB2 and TAB3 
dissociate from Beclin 1 and engage in stimulatory interactions with TAK1. The 
inhibitory interaction between TABs and Beclin 1 is mediated by their 
coiled-coil domains (CCDs). Accordingly, the overexpression of either TAB2 or 
TAB3 CCD stimulates Beclin 1- and TAK1-dependent autophagy. These results point 
to the existence of a direct molecular crosstalk between the canonical NFκB 
activation pathway and the autophagic core machinery that guarantees the 
coordinated induction of these processes in response to stress.