SQSTM1 oligomer is phosphorylated

Stable Identifier
R-HSA-9766532
Type
Reaction [transition]
Species
Homo sapiens
Compartment
cytosol
ReviewStatus
5/5
Locations in the PathwayBrowser
Expand all
General
SVG | 
PNG
Low
Medium
High
 | PPTX  | SBGN
SQSTM1 oligomer is phosphorylated
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
SQSTM1 is phosphorylated at serine 349 by an unknown kinase (Ichimura et al, 2013; reviewed in Jiang et al, 2015; Lamark et al, 2017; Baird and Yamamoto, 2020). This serine residues lies in the STGE motif of SQSTM1 that mediates the interaction with the KELCH1 domain of KEAP1, and phosphorylation increases the strength of the binding. Binding of phosphorylated SQSTM1 to KEAP1 competes with NFE2L2 for the site and consequently stabilizes NFE2L2 (Ichimura et al, 2013; reviewed in Jiang et al, 2015; Lamark et al, 2017; Baird and Yamamoto, 2020).
Literature References
PubMed ID Title Journal Year
32284348 The Molecular Mechanisms Regulating the KEAP1-NRF2 Pathway

Baird, L, Yamamoto, M

Mol Cell Biol 2020
26117325 p62 links autophagy and Nrf2 signaling

Jiang, T, Harder, B, Rojo de la Vega, M, Wong, PK, Chapman, E, Zhang, DD

Free Radic Biol Med 2015
24011591 Phosphorylation of p62 activates the Keap1-Nrf2 pathway during selective autophagy

Ichimura, Y, Waguri, S, Sou, YS, Kageyama, S, Hasegawa, J, Ishimura, R, Saito, T, Yang, Y, Kouno, T, Fukutomi, T, Hoshii, T, Hirao, A, Takagi, K, Mizushima, T, Motohashi, H, Lee, MS, Yoshimori, T, Tanaka, K, Yamamoto, M, Komatsu, M

Mol Cell 2013
29233872 Regulation of selective autophagy: the p62/SQSTM1 paradigm

Lamark, T, Svenning, S, Johansen, T

Essays Biochem 2017
Participants
Input
Output
Participates
as an event of
Catalyst Activity

protein serine/threonine kinase activity of unknown kinase [cytosol]

Physical Entity
unknown kinase [cytosol] (Homo sapiens)
Activity
protein serine/threonine kinase activity (GO:0004674)
Authored
Rothfels, K  (2021-10-08)
Reviewed
Cuadrado, A  (2022-02-23)
Created
Rothfels, K  (2022-02-22)
Cite Us!