in  the  destruction  of  target  proteins,

analogous to our observations regarding

TCR-stimulated  proteolysis  of  BCL10.

Collectively,  these  studies  suggest  that

autophagy  adaptors  are  intimately  con-

nected to both the autophagy and protea-

somal degradation machinery. We expect

that many additional  examples  of selec-

tive autophagy of signaling proteins will  

tude of NFKB1-RELA activation. Thus,

SQSTM1 is paradoxically required both

for  BCL10  activation  of NFKB1-RELA

and  for  limiting  activation  of  NFKB1-

RELAvia directing BCL10 autophagy.

Remarkably,  this  autophagy  process

is highly selective, resulting in degrada-

tion of BCL10, but not its direct binding

partner, MALT1. BCL10 is constitutively

associated  with  MALT1,  an  important

signaling partner (Fig. 1). Unexpectedly,

we found that LC3 interacts with only

BCL10,   and   not   MALT1.   Moreover,

unlike BCL10, MALT1 is not degraded

after T cell activation. Therefore, BCL10