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The receptor-like kinase Suppressor of BIR1 (SOBIR1) binds various receptor-like proteins (RLPs) that perceive microbe-associated molecular patterns (MAMPs) at the plasma membrane, which is thought to activate plant pattern-triggered immunity (PTI) against pathogen invasion. Despite its potentially crucial role, how SOBIR1 transmits immune signaling to ultimately elicit PTI remains largely unresolved. Herein, we report that a Nicotiana benthamiana gene Nb RLP1, like Nb SOBIR1, was highly induced upon Phytophthora parasitica infection. Intriguingly, Nb RLP1 is characterized as a receptor-like protein localizing to the endoplasmic reticulum (ER) membrane rather than the plasma membrane. Using bimolecular fluorescence complementation and affinity purification assays, we established that Nb RLP1 is likely to associate with Nb SOBIR1 through the contact between the ER and plasma membrane. We further found that Nb SOBIR1 at the plasma membrane partitions into mobile microdomains that undergo frequent lateral movement and internalization. Remarkably, the dynamics of Nb SOBIR1 microdomain is coupled to the remodeling of the cortical ER network. When Nb SOBIR1 microdomains were induced by the P. parasitica MAMP ParA1, tobacco cells overexpressing Nb RLP1 accelerated Nb SOBIR1 internalization. Overexpressing Nb RLP1 in tobacco further exaggerated the ParA1-induced necrosis. Together, these findings have prompted us to propose that ER and the ER-localized Nb RLP1 may play a role in transmitting plant immune signals by regulating Nb SOBIR1 internalization. [ABSTRACT FROM AUTHOR]

The receptor-like kinase Suppressor of BIR1 (SOBIR1) binds various receptor-like proteins (RLPs) that perceive microbe-associated molecular patterns (MAMPs) at the plasma membrane, which is thought to activate plant pattern-triggered immunity (PTI) against pathogen invasion. Despite its potentially crucial role, how SOBIR1 transmits immune signaling to ultimately elicit PTI remains largely unresolved. Herein, we report that a Nicotiana benthamiana gene NbRLP1, like NbSOBIR1, was highly induced upon Phytophthora parasitica infection. Intriguingly, NbRLP1 is characterized as a receptor-like protein localizing to the endoplasmic reticulum (ER) membrane rather than the plasma membrane. Using bimolecular fluorescence complementation and affinity purification assays, we established that NbRLP1 is likely to associate with NbSOBIR1 through the contact between the ER and plasma membrane. We further found that NbSOBIR1 at the plasma membrane partitions into mobile microdomains that undergo frequent lateral movement and internalization. Remarkably, the dynamics of NbSOBIR1 microdomain is coupled to the remodeling of the cortical ER network. When NbSOBIR1 microdomains were induced by the P. parasitica MAMP ParA1, tobacco cells overexpressing NbRLP1 accelerated NbSOBIR1 internalization. Overexpressing NbRLP1 in tobacco further exaggerated the ParA1-induced necrosis. Together, these findings have prompted us to propose that ER and the ER-localized NbRLP1 may play a role in transmitting plant immune signals by regulating NbSOBIR1 internalization.

Autophagy is an essential system for degrading and recycling cellular components for survival during starvation conditions. Under sucrose starvation, application of a papain protease inhibitor E-64d to the Arabidopsis root and tobacco BY-2 cells induced the accumulation of vesicles, labeled with a fluorescent membrane marker FM4-64. The E-64d–induced vesicle accumulation was reduced in the mutant defective in autophagy-related genes ATG2 , ATG5 , and ATG7 , suggesting autophagy is involved in the formation of these vesicles. To clarify the formation of these vesicles in detail, we monitored time-dependent changes of tonoplast, and vesicle accumulation in sucrose-starved cells. We found that these vesicles were derived from the tonoplast and produced by microautophagic process. The tonoplast proteins were excluded from the vesicles, suggesting that the vesicles are generated from specific membrane domains. Concanamycin A treatment in GFP-ATG8a transgenic plants showed that not all FM4-64–labeled vesicles, which were derived from the tonoplast, contained the ATG8a-containing structure. These results suggest that ATG8a may not always be necessary for microautophagy. [ABSTRACT FROM AUTHOR]

Lipid bodies (LBs) are universal constituents of both animal and plant cells. They are produced by specialised membrane domains at the tubular endoplasmic reticulum (ER), and consist of a core of neutral lipids and a surrounding monolayer of phospholipid with embedded amphipathic proteins. Although originally regarded as simple depots for lipids, they have recently emerged as organelles that interact with other cellular constituents, exchanging lipids, proteins and signalling molecules, and shuttling them between various intracellular destinations, including the plasmamembrane (PM). Recent data showed that in plants LBs can deliver a subset of 1,3-β-glucanases to the plasmodesmal (PD) channel. We hypothesise that this may represent a more general mechanism, which complements the delivery of GPI-anchored proteins to the PD exterior via the secretory pathway. We propose that LBs may contribute to the maintenance of the PD chamber and the delivery of regulatory molecules as well as proteins destined for transport to adjacent cells. In addition, we speculate that LBs deliver their cargo through interaction with membrane domains in the cytofacial side of the PM.

Although proteins and lipids have been assumed to be distributed homogeneously in the plasma membrane (PM), recent studies suggest that the PM is non-uniform, forming a structure that includes a number of lateral domains enriched in specific components, such as sterols, sphingolipids, and integral and surface-bound proteins. These domains are called microdomains and are considered the platform for biochemical reaction centers involved in various physiological processes. Microdomains can be extracted as detergent-resistant membrane (DRM) fractions, and such fractions have been isolated from some plant species and used for proteomic and other biochemical characterizations to gain understanding of microdomain functions. Profiling sterol-dependent proteins using a putative microdomain-disrupting agent suggests specific lipid-protein interactions in microdomains. Furthermore, in some plant species, DRM proteomes dynamically respond to biotic and abiotic stresses. Taken together, these results suggest that DRM proteomic studies provide important information for understanding microdomain physiological functions that are critical to the successful prosecution of a plant’s life cycle, particularly in its development and stress responses.

Although proteins and lipids have been assumed to be distributed homogeneously in the plasma membrane (PM), recent studies suggest that the PM is in fact non-uniform structure that includes a number of lateral domains enriched in specific components (i.e., sterols, sphingolipids, and some kind of proteins). These domains are called as microdomains and considered to be the platform of biochemical reaction center for various physiological processes. Microdomain is able to be extracted as detergent-resistant membrane (DRM) fractions, and DRM fractions isolated from some plant species have been used for proteome and other biochemical characterizations to understand microdomain functions. Profiling of sterol-dependent proteins using a putative microdomain-disrupting agent suggests specific lipid-protein interactions in the microdomain. Furthermore, DRM proteomes dynamically respond to biotic and abiotic stresses in some plant species. Taken together, these results suggest that DRM proteomic studies provide us important information to understand physiological functions of microdomains that are critical to prosecute plant's life cycle successfully in the aspect of development and stress responses. [ABSTRACT FROM AUTHOR]

Lipid bodies (LBs) are universal constituents of both animal and plant cells. They are produced by specialized membrane domains at the tubular endoplasmic reticulum (ER), and consist of a core of neutral lipids and a surrounding monolayer of phospholipid with embedded amphipathic proteins. Although originally regarded as simple depots for lipids, they have recently emerged as organelles that interact with other cellular constituents, exchanging lipids, proteins and signaling molecules, and shuttling them between various intracellular destinations, including the plasmamembrane (PM). Recent data showed that in plants LBs can deliver a subset of 1,3-β-glucanases to the plasmodesmal (PD) channel. We hypothesize that this may represent a more general mechanism, which complements the delivery of glycosylphosphatidylinositol (GPI)-anchored proteins to the PD exterior via the secretory pathway. We propose that LBs may contribute to the maintenance of the PD chamber and the delivery of regulatory molecules as well as proteins destined for transport to adjacent cells. In addition, we speculate that LBs deliver their cargo through interaction with membrane domains in the cytofacial side of the PM.