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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.

Published byWidya Sugiarto Modified over 5 years ago

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Presentation on theme: "Role of C-terminal phosphorylation in the subcellular localization of AtPIP2;1 in response to salinity. Role of C-terminal phosphorylation in the subcellular."— Presentation transcript:

1 Role of C-terminal phosphorylation in the subcellular localization of AtPIP2;1 in response to salinity. Role of C-terminal phosphorylation in the subcellular localization of AtPIP2;1 in response to salinity. The figure shows typical laser-scanning confocal micrographs of the fluorescence emitted by transgenic root cells located at 1 cm from the apex and expressing GFP-PIP2;1 (A and B), GFP-PIP2;1-S280A (C and D), GFP-PIP2;1-S283A (E and F), or GFP-PIP2;1-S283D (G and H). Plants were treated during 2 h (A, C, E, and G) or 4 h (B, D, F, and H) with 100 mm NaCl prior to microscopic observations. Scale bar, 20 μm. Sodana Prak et al. Mol Cell Proteomics 2008;7: © 2008 The American Society for Biochemistry and Molecular Biology

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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.

Quantification of intracellular fuzzy staining (A) and of spherical bodies (B) in root cells upon an NaCl treatment. Quantification of intracellular fuzzy.
Quantification of C-terminal phosphorylation of AtPIP2;1 upon NaCl (A) and H2O2 (B) treatments.A, plants were either untreated (white bars) or treated.

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.

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

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.

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.

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 1188.53).

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.

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

Role of C-terminal phosphorylation in the subcellular localization of AtPIP2;1.A, the figure shows typical laser-scanning confocal micrographs of the fluorescence.
Phosphorylation and sequence disorder in microtubule-associated protein Tau.A, schematic illustration of the domain profile of Tau with all known phosphorylation.

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,

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 1617.55).

Phosphopeptide sequencing by MALDI-TOF/TOF of the C-terminal tail of AtPIP2;4.A, MS/MS spectrum of singly phosphorylated 277ALGSFGSFGSFRSFA291 (m/z ).
Phosphopeptide sequencing by MALDI-TOF/TOF of the C-terminal tail of AtPIP2;7.A, MS/MS spectrum of singly phosphorylated 270ALGSFRSNATN280 (m/z 1217.53).

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.

Percentage of proteins identified in envelope membrane extracts according to the purification method and the number of transmembrane domains. Percentage.
Novel phosphorylation sites on H+-ATPase proteins

Novel phosphorylation sites on H+-ATPase proteins
Illustration of matched (FL-IFN-γR2/GFP and IFN-γR1/EBFP) and mismatched (IFN-γR1/EBFP and FL-IL-10R2/GFP) pairs of receptors. Illustration of matched.

Illustration of matched (FL-IFN-γR2/GFP and IFN-γR1/EBFP) and mismatched (IFN-γR1/EBFP and FL-IL-10R2/GFP) pairs of receptors. Illustration of matched.
Frequency distribution of the GRAVY of the theoretical proteins (open bars) and of 110 genes encoding proteins identified on a 2-D electrophoresis gel,

Frequency distribution of the GRAVY of the theoretical proteins (open bars) and of 110 genes encoding proteins identified on a 2-D electrophoresis gel,
Distributions of the ELDP values and Mascot scores for all protein identifications.a, frequency of ELDP value returned by correct (gray bars) and incorrect.

Distributions of the ELDP values and Mascot scores for all protein identifications.a, frequency of ELDP value returned by correct (gray bars) and incorrect.
Significantly enriched phosphorylation motifs from up-regulated phosphopeptides by Motif-X analysis. Significantly enriched phosphorylation motifs from.

Significantly enriched phosphorylation motifs from up-regulated phosphopeptides by Motif-X analysis. Significantly enriched phosphorylation motifs from.
Visual validation of the computational outputs.

Visual validation of the computational outputs.

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