2010
DOI: 10.1038/emboj.2010.175
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Spatial organization of transmembrane receptor signalling

Abstract: The spatial organization of transmembrane receptors is a critical step in signal transduction and receptor trafficking in cells. Transmembrane receptors engage in lateral homotypic and heterotypic cis-interactions as well as intercellular trans-interactions that result in the formation of signalling foci for the initiation of different signalling networks. Several aspects of ligand-induced receptor clustering and association with signalling proteins are also influenced by the lipid composition of membranes. Th… Show more

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Cited by 118 publications
(109 citation statements)
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“…When plants are exposed to highammonium conditions, roots undergo a rapid decrease in N-uptake capacity to avoid cellular ammonium toxicity (3). Previous studies reported that the spatial organization of transmembrane proteins is a critical step in signal transduction and protein trafficking, and different multimeric states of the protein complex can result in distinct cellular responses (17). To test whether highammonium stress changes AMT1;3 protein organization, we compared the state of individual AMT1;3-EGFP spots under highammonium stress (30 mM NH 4 + ) and under N-sufficient conditions (2 mM NH 4 + ).…”
Section: Resultsmentioning
confidence: 99%
“…When plants are exposed to highammonium conditions, roots undergo a rapid decrease in N-uptake capacity to avoid cellular ammonium toxicity (3). Previous studies reported that the spatial organization of transmembrane proteins is a critical step in signal transduction and protein trafficking, and different multimeric states of the protein complex can result in distinct cellular responses (17). To test whether highammonium stress changes AMT1;3 protein organization, we compared the state of individual AMT1;3-EGFP spots under highammonium stress (30 mM NH 4 + ) and under N-sufficient conditions (2 mM NH 4 + ).…”
Section: Resultsmentioning
confidence: 99%
“…Thus, they interact with the ligand through their extra-cellular domain, and recruit different components of the transduction machinery in their intra-cellular domain (Figure 2). The cell biology of receptors is complex and diverse, but in general includes mechanisms to ensure the correct trafficking of the receptor through the Endoplasmic reticulum-Golgi network, post-transcriptional modifications during trafficking to synthesize the active form of the protein, localization of the receptor to apical domains in the cell membrane, interaction of the receptor with different co-receptor molecules, and turn-over mechanisms that regulate the number of activated-receptors in the cell membrane and other intracellular compartments (Piddini and Vincent, 2003;Hoeller et al, 2005;Mills, 2007;Sorkin and von Zastrow, 2009;Bethani et al, 2010). Similarly, the activation of the receptor by binding to appropriate ligands uses different mechanisms that rely in the clustering of receptor complexes, phosphorylation of receptor molecules after complex formation (EGFR and TGFß), or conformational changes that allow the proteolytic processing of the receptor (Notch) or its interaction with specific transduction components (Wnt; Figure 2).…”
Section: Introductionmentioning
confidence: 99%
“…10,[25][26][27] From an application point of view, the 2D case is of particular importance in cell biological applications, where it may help shed light on processes such as signal-induced inhomogeneities and receptor clustering on cell membranes. 28 Whereas the practical difference between volume and contact reactivity models may be negligible in terms of the binding probability in 3D, 18 this may be different for the full GF and requires further clarification in the 2D case. GF of the 3D generalized FKE have been obtained in the Laplace domain before.…”
Section: Introductionmentioning
confidence: 99%