Role of C-terminal phosphorylation in the subcellular localization of AtPIP2;1.A, the figure shows typical laser-scanning confocal micrographs of the fluorescence.

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Quantification of intracellular fuzzy staining (A) and of spherical bodies (B) in root cells upon an NaCl treatment. Quantification of intracellular fuzzy.

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Role of C-terminal phosphorylation in the subcellular localization of AtPIP2;1 in response to salinity. Role of C-terminal phosphorylation in the subcellular.

binding sites 58 of the 473 unambiguously assigned phosphorylation sites are predicted by Scansite to be sites for binding. 50 of these correspond.

PLGEM parameters are reasonably stable to decreasing number of replicates. PLGEM parameters are reasonably stable to decreasing number of replicates. A.

Quantification of C-terminal phosphorylation of AtPIP2;1 upon NaCl (A) and H2O2 (B) treatments.A, plants were either untreated (white bars) or treated.

Correlation of log-transformed signal intensity from two Affymetrix microarray hybridizations using platelet RNA. Plotted are those probesets with an average.

Sequence alignment of C-terminal phosphorylated plant aquaporins

Principle for quantification of phosphorylation of the C-terminal tail of AtPIP2;1. Principle for quantification of phosphorylation of the C-terminal tail.

MALDI-TOF MS spectrum of phosphopeptides from plant PM aquaporins.

Phosphopeptide sequencing by MALDI-TOF/TOF of the C-terminal tail of AtPIP2;1.A, MS/MS spectrum of singly phosphorylated 277SLGSFRSAANV287 (m/z ).

Enrichment of sequence disorder in the cytosolic phosphoproteome.

Phosphorylation and sequence disorder in microtubule-associated protein Tau.A, schematic illustration of the domain profile of Tau with all known phosphorylation.

Distribution of phosphorylation sites identified in the cytosolic phosphoproteome.A, numbers of approved phosphopeptides, previously phosphorylated peptides,

Phosphopeptide sequencing by MALDI-TOF/TOF of the C-terminal tail of AtPIP2;4.A, MS/MS spectrum of singly phosphorylated 277ALGSFGSFGSFRSFA291 (m/z ).

Fast protein LC IMAC purification of cytosolic phosphoproteins

Phosphopeptide sequencing by MALDI-TOF/TOF of the C-terminal tail of AtPIP2;7.A, MS/MS spectrum of singly phosphorylated 270ALGSFRSNATN280 (m/z ).

Percentage of proteins identified in envelope membrane extracts according to the purification method and the number of transmembrane domains. Percentage.

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Significantly enriched phosphorylation motifs from up-regulated phosphopeptides by Motif-X analysis. Significantly enriched phosphorylation motifs from.

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Representative example of LAXIC performance for complex plant phosphoproteome. Representative example of LAXIC performance for complex plant phosphoproteome.A.

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Distribution of the phosphoproteins based on GO analysis, including biological process (Left) and cellular component (Right). Distribution of the phosphoproteins.

Examples of protein that display profiles corresponding to GO/GROW and STOP signals.A, example of STOP profile: normalized spot volume profile of apoA-I.

Extraction of proteins from MALDI IMS slides.

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Bar plot representation of the transcriptomic changes in Δsaci_ptp and Δsaci_pp2a. Bar plot representation of the transcriptomic changes in Δsaci_ptp and.

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Changes in mRNA levels do not correlate with changes in protein levels in upf1Δ and xrn1Δ cells. Changes in mRNA levels do not correlate with changes in.

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SiRNA knockdown of dynein IC2-C recovered the inhibition of neurite outgrowth in NF1-KD PC12 cells. siRNA knockdown of dynein IC2-C recovered the inhibition.

Changes in protein expression during distinct stages of NK cell differentiation. Changes in protein expression during distinct stages of NK cell differentiation.

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Comparison of fluorescence spectra of cells expressing the FL-IFN-γR2/EBFP and FL-IFN-γR2/GFP chains in the presence and absence of the IFN-γR1 chain and.

Fig. 7. Analysis of dFMRP kinetics in dFMRP granules by FRAP

Survey of phosphorylation motifs

SlMYB21 Encodes an Active Transcription Factor That Interacts With SlJAZ9 and Complements the Arabidopsis Mutant myb21-5. SlMYB21 Encodes an Active Transcription.

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Model of the change in receptor structure on engagement of the ligand IFN-γ. Model of the change in receptor structure on engagement of the ligand IFN-γ.

Presentation transcript:

Role of C-terminal phosphorylation in the subcellular localization of AtPIP2;1.A, the figure shows typical laser-scanning confocal micrographs of the fluorescence emitted by root epidermal cells at 1 cm from the apex in transgenic plants that express GFP-PIP2;1, GFP-PIP2;1-S280A, GFP-PIP2;1-S283A, or GFP-PIP2;1-S283D. Role of C-terminal phosphorylation in the subcellular localization of AtPIP2;1.A, the figure shows typical laser-scanning confocal micrographs of the fluorescence emitted by root epidermal cells at 1 cm from the apex in transgenic plants that express GFP-PIP2;1, GFP-PIP2;1-S280A, GFP-PIP2;1-S283A, or GFP-PIP2;1-S283D. Scale bar, 20 μm. B, the graph represents the proportion of root cells at 1 cm from the apex with an intracellular staining. Data were obtained from transgenic plants that express the following constructs: GFP-PIP2;1 (n = 13 plants from two independent transgenic lines), GFP-PIP2;1-S280A (n = 9 plants from three independent transgenic lines), GFP-PIP2;1-S283A (n = 7 plants from two independent transgenic lines), and GFP-PIP2;1-S283D (n = 6 plants from two independent transgenic lines). The numbers on the graph correspond to the total number of observed cells. The error bars represent S.D. Sodana Prak et al. Mol Cell Proteomics 2008;7:1019-1030 © 2008 The American Society for Biochemistry and Molecular Biology