Remove, Recycle, Degrade: Regulating Plasma Membrane Protein Accumulation

Abstract

Interactions between plant cells and the environment rely on modulation of protein receptors, transporters, channels, and lipids at the plasma membrane (PM) to facilitate intercellular communication, nutrient uptake, environmental sensing, and directional growth. These functions are fine-tuned by cellular pathways maintaining or reducing particular proteins at the PM. Proteins are endocytosed, and their fate is decided between recycling and degradation to modulate localization, abundance, and activity. Selective autophagy is another pathway regulating PM protein accumulation in response to specific conditions or developmental signals. The mechanisms regulating recycling, degradation, and autophagy have been studied extensively, yet we are just now addressing their regulation and coordination. Here, we (1) provide context concerning regulation of protein accumulation, recycling, or degradation by overviewing endomembrane trafficking; (2) discuss pathways regulating recycling and degradation in terms of cellular roles and cargoes; (3) review plant selective autophagy and its physiological significance; (4) focus on two decision-making mechanisms: regulation of recycling versus degradation of PM proteins and coordination between autophagy and vacuolar degradation; and (5) identify future challenges.

Subcellular Journey of Rare Cold Inducible 2 Protein in Plant Under Stressful Condition

“…Endocytosis is a basic metabolism in living organism that participating remove, recycle, and degrade of proteins from PM ( Rodriguez-Furlan et al, 2019 ). It maintains cell homeostasis by fine-tuning the PM system to adapt to biotic and abiotic stresses in plants ( Wang et al, 2020 ).…”

Membrane dynamics during individual and combined abiotic stresses in plants and tools to study the same

“…For example, to survive at low temperatures, plants tend to increase the DBI index of membrane lipids (Zhang et al 2019). Furthermore, PM‐bound proteins, including sensors, receptors, channels, transporters, also modulate the plant–environment interactions and facilitate the environmental sensing, intercellular communication as well as nutrient, ion and water transport in response to external stimuli (Rodriguez‐Furlan et al 2019). In response to various environmental adversities, membrane lipids regulate the activity and localization of the membrane proteins to improve the stress adaptation ability of plants (Liu X et al 2019).…”

Regulation of Three Key Kinases of Brassinosteroid Signaling Pathway

“…Endocytosed BRI1 proteins accumulate in the TGN/EE compartments where they are sorted into the vacuole for degradation, an endocytic pathway that is mediated through sorting/packaging of BRI1 into ILVs (intraluminal vesicles) of the LE/MVBs (late endosomes/multivesicular bodies) and eventual MVB-vacuole fusion [ 111 ]. Previous studies suggested that BRI1 endocytosis and its subsequent sorting at TGN/EE into MVBs is likely regulated by the E3 ligases PUB12/13 (plant U-box protein12/13)-catalyzed ubiquitination of BRI1 [ 112 ] while its packaging into MVBs is regulated by ESCRT protein complexes and their associated proteins [ 113 ].…”

“…Most of the endocytosed BRI1 are thought to be recycled back to the PM to replenish the PM pool of the BR receptor, thus enhancing BR signaling [ 99 , 101 , 102 , 104 ]. It was thought that the TGN/EE-PM recycling involves retromer complex-mediated cargo retrieval, microtubule-assisted trafficking of recycling endosomes, and SNARE (soluble N-ethylmaleimide-sensitive factor attachment proteins receptor)-mediated exocytosis [ 111 ]. A hypomorphic allele of DET3 that encodes the cytosolic C subunit of the Arabidopsis vacuolar ATPase (V-ATPase) reduces the ability of V-ATPase to acidify the TGN/EE but not the Golgi or the vacuole, leading to compromised secretion and recycling of BRI1 and reduced BR sensitivity [ 120 , 121 ].…”