Signaling through C2 domains: More than one lipid target

Corbalán-Garcı́a, Senena; Gómez‐Fernández, Juan C.

doi:10.1016/j.bbamem.2014.01.008

Cited by 196 publications

(218 citation statements)

References 128 publications

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“…This arrangement keeps the lipid chains embedded in the membrane while the protein interacts with the phosphoglyceride headgroup. LBDs help target and tether various peripheral amphitropic proteins to select intracellular membrane sites (22)(23)(24)(25)(26)(27). Our experimental data support the idea of POPS functioning as a membrane tethering site that helps orient ACD11 and CPTP in ways that optimize function.…”

Section: Journal Of Biological Chemistry 2535supporting

confidence: 74%

“…ACD11, CPTP, and GLTP are considered to be amphitropic proteins because their functionality involves translocation on/off membranes to bind and release the sphingolipid cargo (19 -21). Amphitropic proteins often contain so-called lipid binding domains (LBDs) that bind specific phosphoglyceride headgroups within membranes to help target and tether to select cell membrane destinations (22)(23)(24)(25)(26)(27). LBDs, such as the C1, C2, PH, PX, and FYVE domains, differ structurally from the GLTP-fold.…”

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confidence: 99%

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Phosphatidylserine Stimulates Ceramide 1-Phosphate (C1P) Intermembrane Transfer by C1P Transfer Proteins

Zhai

Gao

Mishra

et al. 2017

Journal of Biological Chemistry

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Edited by George M. CarmanGenetic models for studying localized cell suicide that halt the spread of pathogen infection and immune response activation in plants include Arabidopsis accelerated-cell-death 11 mutant (acd11). In this mutant, sphingolipid homeostasis is disrupted via depletion of ACD11, a lipid transfer protein that is specific for ceramide 1-phosphate (C1P) and phyto-C1P. The C1P binding site in ACD11 and in human ceramide-1-phosphate transfer protein (CPTP) is surrounded by cationic residues. Here, we investigated the functional regulation of ACD11 and CPTP by anionic phosphoglycerides and found that 1-palmitoyl-2-oleoyl-phosphatidic acid or 1-palmitoyl-2-oleoyl-phosphatidylglycerol (<15 mol %) in C1P source vesicles depressed C1P intermembrane transfer. By contrast, replacement with 1-palmitoyl-2-oleoyl-phosphatidylserine stimulated C1P transfer by ACD11 and CPTP. Notably, "soluble" phosphatidylserine (dihexanoyl-phosphatidylserine) failed to stimulate C1P transfer. Also, none of the anionic phosphoglycerides affected transfer action by human glycolipid lipid transfer protein (GLTP), which is glycolipid-specific and has few cationic residues near its glycolipid binding site. These findings provide the first evidence for a potential phosphoglyceride headgroup-specific regulatory interaction site(s) existing on the surface of any GLTP-fold and delineate new differences between GLTP superfamily members that are specific for C1P versus glycolipid.

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Section: Journal Of Biological Chemistry 2535supporting

confidence: 74%

mentioning

confidence: 99%

Phosphatidylserine Stimulates Ceramide 1-Phosphate (C1P) Intermembrane Transfer by C1P Transfer Proteins

Zhai

Gao

Mishra

et al. 2017

Journal of Biological Chemistry

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“…Little is known about the membrane binding properties of these proteins, especially those features related to the molecular mechanism underlying their lipid specificity. This relies on the structure and amino acid composition of the canonical Ca 2+ -dependent and the polybasic lipid binding sites (39)(40)(41). The binding of C2 domains through the latter determines the orientation of the domain with respect to the membrane.…”

Section: Resultsmentioning

confidence: 99%

Calcium-dependent oligomerization of CAR proteins at cell membrane modulates ABA signaling

Díaz

Sánchez-Barrena

González-Rubio

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

110

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Regulation of ion transport in plants is essential for cell function. Abiotic stress unbalances cell ion homeostasis, and plants tend to readjust it, regulating membrane transporters and channels. The plant hormone abscisic acid (ABA) and the second messenger Ca 2+ are central in such processes, as they are involved in the regulation of protein kinases and phosphatases that control ion transport activity in response to environmental stimuli. The identification and characterization of the molecular mechanisms underlying the effect of ABA and Ca 2+ signaling pathways on membrane function are central and could provide opportunities for crop improvement. The C2-domain ABA-related (CAR) family of small proteins is involved in the Ca 2+ -dependent recruitment of the pyrabactin resistance 1/PYR1-like (PYR/PYL) ABA receptors to the membrane. However, to fully understand CAR function, it is necessary to define a molecular mechanism that integrates Ca 2+ sensing, membrane interaction, and the recognition of the PYR/PYL interacting partners. We present structural and biochemical data showing that CARs are peripheral membrane proteins that functionally cluster on the membrane and generate strong positive membrane curvature in a Ca 2+ -dependent manner. These features represent a mechanism for the generation, stabilization, and/or specific recognition of membrane discontinuities. Such structures may act as signaling platforms involved in the recruitment of PYR/PYL receptors and other signaling components involved in cell responses to stress.signaling | ion transport | membrane biology | abiotic stress M any of the plant-adaptive responses to environmental stresses occur at the cell membrane. In particular, those related to the regulation of plant ion transporters as stress unbalance cell ion homeostasis (1, 2). The phytohormone abcisic acid (ABA) and the second messenger Ca 2+ have central roles in regulating plant stress tolerance through the control of the activity of various families of protein kinases and phosphatases that regulate the activation of different ion channels or transporters (3-7). Given the presence of the channel substrates at the cell membranes and the transient nature of their activation, the functioning of these systems relies on the regulated localization of different molecular entities in the vicinity of the channels via protein-protein (8, 9) and/or protein-membrane interactions (10, 11).The pyrabactin resistance 1/PYR1-like (PYR/PYL)/regulatory components of ABA receptors (RCAR) receptors perceive intracellular ABA levels and, as a result, form ternary complexes with clade A protein phosphatases type 2C (PP2C), thereby inactivating them (12)(13)(14)(15). This prevents the PP2C-mediated dephosphorylation of ABA-activated sucrose nonfermenting 1-related protein kinases (SnRKs) subfamily 2 (SnRK2s), which results in the activation of an SnRK2-dependent phosphorylation cascade affecting a high number of targets in the plant cell (16,17). As a result, ABA-activated SnRK2s are key players in regulating...

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“…(Fig. 2, bottom left) Most of the proteins that contain C 2 -domains are involved in either signal transduction pathways or membrane traffic (32). Among the best studied C 2 proteins is synaptotagmin, a transmembrane protein that contains two such domains.…”

Section: Other Calcium-binding Motifs In Proteinsmentioning

confidence: 99%

Why Calcium? How Calcium Became the Best Communicator

Carafoli

Krebs

2016

Journal of Biological Chemistry

305

213

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Calcium carries messages to virtually all important functions of cells. Although it was already active in unicellular organisms, its role became universally important after the transition to multicellular life. In this Minireview, we explore how calcium ended up in this privileged position. Most likely its unique coordination chemistry was a decisive factor as it makes its binding by complex molecules particularly easy even in the presence of large excesses of other cations, e.g. magnesium. Its free concentration within cells can thus be maintained at the very low levels demanded by the signaling function. A large cadre of proteins has evolved to bind or transport calcium. They all contribute to buffer it within cells, but a number of them also decode its message for the benefit of the target. The most important of these "calcium sensors" are the EF-hand proteins. Calcium is an ambivalent messenger. Although essential to the correct functioning of cell processes, if not carefully controlled spatially and temporally within cells, it generates variously severe cell dysfunctions, and even cell death.At the beginning, life on earth consisted of single cells that were capable of carrying out all vital functions. The interplay with other cells was largely limited to the competition for nutrients. Unicellularity was clearly successful, as shown by the fact that unicellular organisms are actually still predominant today. Nevertheless, at a time which was generally estimated to be at 600 -700 million years ago, but which is now being pushed back to more than 2 billion years ago (1, 2), competition was replaced by cooperation, and multicellular life evolved. It had somehow become advantageous for cells to work together rather than to live alone. Cells became gradually organized into structures in which they learned to perform different tasks and to cooperate in the division of labor. Cooperation naturally demanded the communication of cells with each other, i.e. it demanded the development of agents that could exchange messages between cells. As the complexity of the multicellular organization increased, so did the number of cells with distinct functional tasks. The number of intercellular signaling molecules and the degree of their complexity increased in parallel. A basic tenet of life is regulation. Thus, all vital functions within the cells are regulated. Indeed, they are also regulated in unicellular organisms. However, the transition to multicellular life brought with it the intercellular exchange of messages as an additional, and essential, regulation category.Calcium, the third most abundant metal in nature, was amply available to cells from the beginning, and was adopted as a regulator at an early evolutionary stage. The basic principles of calcium regulation were already present in prokaryotes and protists (3, 4), but calcium regulation gradually grew to cover nearly all aspects of cell function after the transition to multicellularity. Naturally, agents that carry messages to intracellular targets must be maint...

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Signaling through C2 domains: More than one lipid target

Cited by 196 publications

References 128 publications

Phosphatidylserine Stimulates Ceramide 1-Phosphate (C1P) Intermembrane Transfer by C1P Transfer Proteins

Phosphatidylserine Stimulates Ceramide 1-Phosphate (C1P) Intermembrane Transfer by C1P Transfer Proteins

Calcium-dependent oligomerization of CAR proteins at cell membrane modulates ABA signaling

Why Calcium? How Calcium Became the Best Communicator

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