ATG8 Expansion: A Driver of Selective Autophagy Diversification?. (March 2017)
- Record Type:
- Journal Article
- Title:
- ATG8 Expansion: A Driver of Selective Autophagy Diversification?. (March 2017)
- Main Title:
- ATG8 Expansion: A Driver of Selective Autophagy Diversification?
- Authors:
- Kellner, Ronny
De la Concepcion, Juan Carlos
Maqbool, Abbas
Kamoun, Sophien
Dagdas, Yasin F. - Abstract:
- Abstract : Selective autophagy is a conserved homeostatic pathway that involves engulfment of specific cargo molecules into specialized organelles called autophagosomes. The ubiquitin-like protein ATG8 is a central player of the autophagy network that decorates autophagosomes and binds to numerous cargo receptors. Although highly conserved across eukaryotes, ATG8 diversified from a single protein in algae to multiple isoforms in higher plants. We present a phylogenetic overview of 376 ATG8 proteins across the green plant lineage that revealed family-specific ATG8 clades. Because these clades differ in fixed amino acid polymorphisms, they provide a mechanistic framework to test whether distinct ATG8 clades are functionally specialized. We propose that ATG8 expansion may have contributed to the diversification of selective autophagy pathways in plants. Trends: Selective autophagy is an ancient membrane-trafficking pathway that is essential for cellular homeostasis. Selective autophagy involves engulfment of autophagic cargo within double-membrane vesicles called autophagosomes. Autophagosomes are decorated by ATG8, a ubiquitin-like protein conserved across eukaryotes that is expanded in higher plants. Selective cargo recruitment is mediated by autophagy receptors that interact with ATG8 via an ATG8 interaction motif (AIM). Specialization of autophagy receptors toward ATG8 variants contributes to selective autophagy. Although selective autophagy plays important roles inAbstract : Selective autophagy is a conserved homeostatic pathway that involves engulfment of specific cargo molecules into specialized organelles called autophagosomes. The ubiquitin-like protein ATG8 is a central player of the autophagy network that decorates autophagosomes and binds to numerous cargo receptors. Although highly conserved across eukaryotes, ATG8 diversified from a single protein in algae to multiple isoforms in higher plants. We present a phylogenetic overview of 376 ATG8 proteins across the green plant lineage that revealed family-specific ATG8 clades. Because these clades differ in fixed amino acid polymorphisms, they provide a mechanistic framework to test whether distinct ATG8 clades are functionally specialized. We propose that ATG8 expansion may have contributed to the diversification of selective autophagy pathways in plants. Trends: Selective autophagy is an ancient membrane-trafficking pathway that is essential for cellular homeostasis. Selective autophagy involves engulfment of autophagic cargo within double-membrane vesicles called autophagosomes. Autophagosomes are decorated by ATG8, a ubiquitin-like protein conserved across eukaryotes that is expanded in higher plants. Selective cargo recruitment is mediated by autophagy receptors that interact with ATG8 via an ATG8 interaction motif (AIM). Specialization of autophagy receptors toward ATG8 variants contributes to selective autophagy. Although selective autophagy plays important roles in development and stress tolerance, the molecular mechanisms underlying selectivity are currently elusive in plants. … (more)
- Is Part Of:
- Trends in plant science. Volume 22:Number 3(2017)
- Journal:
- Trends in plant science
- Issue:
- Volume 22:Number 3(2017)
- Issue Display:
- Volume 22, Issue 3 (2017)
- Year:
- 2017
- Volume:
- 22
- Issue:
- 3
- Issue Sort Value:
- 2017-0022-0003-0000
- Page Start:
- 204
- Page End:
- 214
- Publication Date:
- 2017-03
- Subjects:
- selective autophagy -- plants -- evolution -- ATG8 -- cargo receptor -- autophagosome
Botany -- Periodicals
Botanique -- Périodiques
Botany
Periodicals
580.5 - Journal URLs:
- http://www.sciencedirect.com/science/journal/13601385 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.tplants.2016.11.015 ↗
- Languages:
- English
- ISSNs:
- 1360-1385
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 9049.675450
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 8835.xml