Regulation of SQSTM1/p62 via UBA domain ubiquitination and its role in disease

You Jin Lee; Conrad C. Weihl

doi:10.1080/15548627.2017.1339845

Regulation of SQSTM1/p62 via UBA domain ubiquitination and its role in disease

You Jin Lee
, Conrad C. Weihl

Research output: Contribution to journal › Comment/debate

54 Scopus citations

Abstract

Macroautophagy/autophagy can be a selective degradative process via the utilization of various autophagic receptor proteins. Autophagic receptors selectively recognize ubiquitinated cargoes and deliver them to phagophores, the precursors to autophagosomes, for their degradation. For example, SQSTM1/p62 directly binds to ubiquitinated protein aggregates via its UBA domain and sequesters them into inclusion bodies via its PB1 domain. SQSTM1also interacts with phagophores via its LC3-interacting (LIR) motif. However, a regulatory mechanism for autophagic receptors is not yet understood.

Original language	English
Pages (from-to)	1615-1616
Number of pages	2
Journal	Autophagy
Volume	13
Issue number	9
DOIs	https://doi.org/10.1080/15548627.2017.1339845
State	Published - Sep 2 2017

Keywords

Keap1-Cullin3-Nrf2 pathway
autophagy
neurodegenerative diseases
p62/SQSTM1
protein aggregates
ubiquitination

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10.1080/15548627.2017.1339845

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title = "Regulation of SQSTM1/p62 via UBA domain ubiquitination and its role in disease",

abstract = "Macroautophagy/autophagy can be a selective degradative process via the utilization of various autophagic receptor proteins. Autophagic receptors selectively recognize ubiquitinated cargoes and deliver them to phagophores, the precursors to autophagosomes, for their degradation. For example, SQSTM1/p62 directly binds to ubiquitinated protein aggregates via its UBA domain and sequesters them into inclusion bodies via its PB1 domain. SQSTM1also interacts with phagophores via its LC3-interacting (LIR) motif. However, a regulatory mechanism for autophagic receptors is not yet understood.",

keywords = "Keap1-Cullin3-Nrf2 pathway, autophagy, neurodegenerative diseases, p62/SQSTM1, protein aggregates, ubiquitination",

author = "Lee, \{You Jin\} and Weihl, \{Conrad C.\}",

note = "Publisher Copyright: {\textcopyright} 2017 Taylor \& Francis.",

year = "2017",

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doi = "10.1080/15548627.2017.1339845",

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AU - Lee, You Jin

AU - Weihl, Conrad C.

PY - 2017/9/2

Y1 - 2017/9/2

N2 - Macroautophagy/autophagy can be a selective degradative process via the utilization of various autophagic receptor proteins. Autophagic receptors selectively recognize ubiquitinated cargoes and deliver them to phagophores, the precursors to autophagosomes, for their degradation. For example, SQSTM1/p62 directly binds to ubiquitinated protein aggregates via its UBA domain and sequesters them into inclusion bodies via its PB1 domain. SQSTM1also interacts with phagophores via its LC3-interacting (LIR) motif. However, a regulatory mechanism for autophagic receptors is not yet understood.

AB - Macroautophagy/autophagy can be a selective degradative process via the utilization of various autophagic receptor proteins. Autophagic receptors selectively recognize ubiquitinated cargoes and deliver them to phagophores, the precursors to autophagosomes, for their degradation. For example, SQSTM1/p62 directly binds to ubiquitinated protein aggregates via its UBA domain and sequesters them into inclusion bodies via its PB1 domain. SQSTM1also interacts with phagophores via its LC3-interacting (LIR) motif. However, a regulatory mechanism for autophagic receptors is not yet understood.

KW - Keap1-Cullin3-Nrf2 pathway

KW - autophagy

KW - neurodegenerative diseases

KW - p62/SQSTM1

KW - protein aggregates

KW - ubiquitination

UR - https://www.scopus.com/pages/publications/85027532274

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DO - 10.1080/15548627.2017.1339845

M3 - Comment/debate

C2 - 28812433

AN - SCOPUS:85027532274

SN - 1554-8627

VL - 13

SP - 1615

EP - 1616

JO - Autophagy

JF - Autophagy

IS - 9

ER -

Regulation of SQSTM1/p62 via UBA domain ubiquitination and its role in disease

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