Knowns and unknowns of plasma membrane protein degradation in plants. (July 2018)
- Record Type:
- Journal Article
- Title:
- Knowns and unknowns of plasma membrane protein degradation in plants. (July 2018)
- Main Title:
- Knowns and unknowns of plasma membrane protein degradation in plants
- Authors:
- Liu, Chuanliang
Shen, Wenjin
Yang, Chao
Zeng, Lizhang
Gao, Caiji - Abstract:
- Highlights: Several plant PM proteins undergo an endocytic pathway to vacuole for degradation. More and more regulators involved in control of PM protein homeostasis are identified. The role of autophagy in PM protein turnover was recently noticed in plants. Abstract: Plasma membrane (PM) not only creates a physical barrier to enclose the intracellular compartments but also mediates the direct communication between plants and the ever-changing environment. A tight control of PM protein homeostasis by selective degradation is thus crucial for proper plant development and plant-environment interactions. Accumulated evidences have shown that a number of plant PM proteins undergo clathrin-dependent or membrane microdomain-associated endocytic routes to vacuole for degradation in a cargo-ubiquitination dependent or independent manner. Besides, several trans-acting determinants involved in the regulation of endocytosis, recycling and multivesicular body-mediated vacuolar sorting have been identified in plants. More interestingly, recent findings have uncovered the participation of selective autophagy in PM protein turnover in plants. Although great progresses have been made to identify the PM proteins that undergo dynamic changes in subcellular localizations and to explore the factors that control the membrane protein trafficking, several questions remain to be answered regarding the molecular mechanisms of PM protein degradation in plants. In this short review article, we brieflyHighlights: Several plant PM proteins undergo an endocytic pathway to vacuole for degradation. More and more regulators involved in control of PM protein homeostasis are identified. The role of autophagy in PM protein turnover was recently noticed in plants. Abstract: Plasma membrane (PM) not only creates a physical barrier to enclose the intracellular compartments but also mediates the direct communication between plants and the ever-changing environment. A tight control of PM protein homeostasis by selective degradation is thus crucial for proper plant development and plant-environment interactions. Accumulated evidences have shown that a number of plant PM proteins undergo clathrin-dependent or membrane microdomain-associated endocytic routes to vacuole for degradation in a cargo-ubiquitination dependent or independent manner. Besides, several trans-acting determinants involved in the regulation of endocytosis, recycling and multivesicular body-mediated vacuolar sorting have been identified in plants. More interestingly, recent findings have uncovered the participation of selective autophagy in PM protein turnover in plants. Although great progresses have been made to identify the PM proteins that undergo dynamic changes in subcellular localizations and to explore the factors that control the membrane protein trafficking, several questions remain to be answered regarding the molecular mechanisms of PM protein degradation in plants. In this short review article, we briefly summarize recent progress in our understanding of the internalization, sorting and degradation of plant PM proteins. More specifically, we focus on discussing the elusive aspects underlying the pathways of PM protein degradation in plants. … (more)
- Is Part Of:
- Plant science. Volume 272(2018)
- Journal:
- Plant science
- Issue:
- Volume 272(2018)
- Issue Display:
- Volume 272, Issue 2018 (2018)
- Year:
- 2018
- Volume:
- 272
- Issue:
- 2018
- Issue Sort Value:
- 2018-0272-2018-0000
- Page Start:
- 55
- Page End:
- 61
- Publication Date:
- 2018-07
- Subjects:
- Autophagy -- Degradation -- Plasma membrane protein -- Recycling -- Ubiquitination
Botany -- Periodicals
Botanique -- Périodiques
580 - Journal URLs:
- http://www.sciencedirect.com/science/journal/01689452 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.plantsci.2018.04.008 ↗
- Languages:
- English
- ISSNs:
- 0168-9452
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6523.390000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 10602.xml