Abstract
p62/SQSTM1 is a stress-inducible cellular protein that is conserved among metazoans but not in plants and fungi. p62/SQSTM1 has multiple domains that mediate its interactions with various binding partners and it serves as a signaling hub for diverse cellular events such as amino acid sensing and the oxidative stress response. In addition, p62/SQSTM1 functions as a selective autophagy receptor for degradation of ubiqutinated substrates. In the present review, we describe the current knowledge about p62 with regard to mammalian target of rapamycin complex 1 activation, the Keap1-Nrf2 pathway and selective autophagy.
Keywords:
Keap1-Nrf2 system; mTORC1; p62/Sqstm1; selective autophagy; ubiquitination.
© 2015 FEBS.
Publication types
-
Research Support, Non-U.S. Gov't
-
Review
MeSH terms
-
Adaptor Proteins, Signal Transducing / chemistry
-
Adaptor Proteins, Signal Transducing / metabolism*
-
Animals
-
Autophagy*
-
Enzyme Activation
-
Humans
-
Intracellular Signaling Peptides and Proteins / agonists
-
Intracellular Signaling Peptides and Proteins / metabolism
-
Kelch-Like ECH-Associated Protein 1
-
Mechanistic Target of Rapamycin Complex 1
-
Models, Biological*
-
Models, Molecular*
-
Multiprotein Complexes / agonists
-
Multiprotein Complexes / metabolism
-
NF-E2-Related Factor 2 / agonists
-
NF-E2-Related Factor 2 / metabolism
-
Protein Interaction Domains and Motifs
-
Sequestosome-1 Protein
-
Signal Transduction*
-
TOR Serine-Threonine Kinases / metabolism
Substances
-
Adaptor Proteins, Signal Transducing
-
Intracellular Signaling Peptides and Proteins
-
KEAP1 protein, human
-
Kelch-Like ECH-Associated Protein 1
-
Multiprotein Complexes
-
NF-E2-Related Factor 2
-
NFE2L2 protein, human
-
SQSTM1 protein, human
-
Sequestosome-1 Protein
-
Mechanistic Target of Rapamycin Complex 1
-
TOR Serine-Threonine Kinases