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289 results for “phosphatases”

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zenodo36/100

Figure 3 of 'Structural basis for the specificity of PPM1H phosphatase for Rab GTPases'

Raw data for Figure 3 from manuscript 'Structural basis for the specificity of PPM1H phosphatase for Rab GTPases', Dieter Waschbüsch, Kerryn Berndsen, Pawel Lis, Axel Knebel, Yuko P. Y. Lam, Dario R. Alessi, Amir R. Khan   Figure 3B-WT.afe7 Astra data file with data shown in Fig.3B (left)   Figure 3B-2Glu.afe7 Astra data file with data shown in Fig.3B (right)   Figure 3C gel.tif: Coomassie stained gel of recombinant PPM1H WT and mutant proteins shown in Fig.3C   Figure 3D Malachite.xlsx: Numerical data for the charts shown in Fig.3D

opencc-by-4.0Jun 2021View details →

zenodo36/100

Figure 2 of 'Structural basis for the specificity of PPM1H phosphatase for Rab GTPases'

Raw data for Figure 2 from manuscript 'Structural basis for the specificity of PPM1H phosphatase for Rab GTPases', Dieter Waschbüsch, Kerryn Berndsen, Pawel Lis, Axel Knebel, Yuko P. Y. Lam, Dario R. Alessi, Amir R. Khan Figure 2A gel.tif: Coomassie-stained SDS-PAGE gel showing the result of crosslinking of PPM1H D288A with phospho-Rab8A.   Figure 2BC. List of cross-links with distances.xlsx: List of crosslinks identified between PPM1H D288A with phospho-Rab8A shown in Fig.2B and Fig.2C.   Figure 2DEF Malachite.xlsx: Numerical data for the charts shown in Fig.2D, Fig.2E and Fig.2F.

opencc-by-4.0Jun 2021View details →

zenodo36/100

Figure EV1 of 'Structural basis for the specificity of PPM1H phosphatase for Rab GTPases'

Raw data for Figure EV1 from manuscript 'Structural basis for the specificity of PPM1H phosphatase for Rab GTPases', Dieter Waschbüsch, Kerryn Berndsen, Pawel Lis, Axel Knebel, Yuko P. Y. Lam, Dario R. Alessi, Amir R. Khan Figure EV1A 700.tif: Top to bottom: <ol> <li>Total LRRK2 blot shown in Fig.EV1A</li> <li>GAPDH loading controls for blots in Fig.EV1A</li> <li>HA blot for Rab10 shown in Fig.EV1A</li> </ol> Figure EV1A 800.tif: <ol> <li>HA blot for PPM phosphatases (PPM constructs) shown In Fig.EV1A</li> <li>Phospho-Rab10 Thr72 blot shown in Fig.EV1A</li> </ol> Figure EV1B.tif: Scans of Coomassie stained gels shown in Fig.EV1B

opencc-by-4.0Jun 2021View details →

zenodo36/100

Figure 6 of 'Structural basis for the specificity of PPM1H phosphatase for Rab GTPases'

Raw data for Figure 6 from manuscript 'Structural basis for the specificity of PPM1H phosphatase for Rab GTPases', Dieter Waschbüsch, Kerryn Berndsen, Pawel Lis, Axel Knebel, Yuko P. Y. Lam, Dario R. Alessi, Amir R. Khan   Figure 6B 700.tif: Top to bottom: <ol> <li>Total LRRK2 blot shown in Fig.6B</li> <li>HA blot for PPM phosphatases (PPM constructs) shown In Fig.6B</li> <li>GAPDH loading controls for blots in Fig.6B</li> <li>HA blot for Rab10 shown in Fig.6B</li> </ol>   Figure 6B 800.tif: <ol> <li>Phospho-Rab10 Thr73 blot shown in Fig.6B</li> </ol>

opencc-by-4.0Jun 2021View details →

zenodo36/100

Figure 1 of 'Structural basis for the specificity of PPM1H phosphatase for Rab GTPases'

Raw data for Figure 1 from manuscript 'Structural basis for the specificity of PPM1H phosphatase for Rab GTPases', Dieter Waschbüsch, Kerryn Berndsen, Pawel Lis, Axel Knebel, Yuko P. Y. Lam, Dario R. Alessi, Amir R. Khan Figure 1D Rab8A.tif: Scans of Coomassie stained gels shown in Fig.1D: Left: Coomassie stained Phos-tag gel of PPM1H with Rab8A Right: Coomassie stained Phos-tag gel of PPM1J with Rab8A   Figure 1D Rab10.tif: Scans of Coomassie stained gels shown in Fig.1D: Upper gel: Coomassie stained Phos-tag gel of PPM1H with Rab10 Lower gel: Coomassie stained Phos-tag gel of PPM1J with Rab10

opencc-by-4.0Jun 2021View details →

zenodo36/100

Figure 5 of 'Structural basis for the specificity of PPM1H phosphatase for Rab GTPases'

Raw data for Figure 5 from manuscript 'Structural basis for the specificity of PPM1H phosphatase for Rab GTPases', Dieter Waschbüsch, Kerryn Berndsen, Pawel Lis, Axel Knebel, Yuko P. Y. Lam, Dario R. Alessi, Amir R. Khan Figure 5BE Malachite.xlsx: Numerical data for the charts shown in Fig.5B and Fig.5E.   Figure 5C.tif: Coomassie stained gel of recombinant PPM1H WT and mutant proteins shown in Fig.5C   Figure 5D 700.png: Top to bottom: 1) Total LRRK2 blot shown in Fig.5D 2) HA blot for PPM phosphatases (PPM constructs) shown in Fig.5D 3) GAPDH loading control for blots in Fig.5D 4) HA blot for Rab10 shown in Fig.5D   Figure 5D 800.png: 1) Phospho-Rab10 pThr73 blot shown in Fig.5D   Figure 5E.tif: Coomassie stained gel of recombinant PPM1H WT and mutant proteins shown in Fig.5E   Figure 5F 700 Rab8A.png: Top to bottom (Rab8A) 1) Total LRRK2 blot shown in Fig.5F 2) HA blot for PPM phosphatases (PPM constructs) shown in Fig.5F 3) GAPDH loading control for blots in Fig.5F 4) HA blot for Rab8A shown in Fig.5F   Figure 5F 800 Rab8A.png: 1) Phospho-Rab8A pThr72 blot shown in Fig.5F   Figure 5F 700 Rab10.png: Top to bottom (Rab10) 1) Total LRRK2 blot shown in Fig.5F 2) HA blot for PPM phosphatases (PPM constructs) shown in Fig.5F 3) GAPDH loading control for blots in Fig.5F 4) HA blot for Rab10 shown in Fig.5F   Figure 5F 800 Rab10.png: 1) Phospho-Rab10 pThr73 blot shown in Fig.5F

opencc-by-4.0Jun 2021View details →

zenodo36/100

Structural basis for the specificity of PPM1H phosphatase for Rab GTPases

LRRK2 serine/threonine kinase is associated with inherited Parkinson’s disease. LRRK2 phosphorylates a subset of Rab GTPases within their switch 2 motif to control their interactions with effectors. Recent work has shown that the metal-dependent protein phosphatase PPM1H counteracts LRRK2 by dephosphorylating Rabs. PPM1H is highly selective and closely related PPM1J exhibits no activity toward substrates such as Rab8a phosphorylated at Thr72 (pThr72). Here we have identified the structural determinant of PPM1H specificity for Rabs. The crystal structure of PPM1H reveals that it is a dimer, confirmed by biophysical analysis, and possesses a conserved catalytic domain that strikingly has evolved a 110-residue flap domain adjacent to the active site. The flap domain distantly resembles tudor domains that interact with histones in the context of epigenetics. Cellular assays, crosslinking and 3-D modelling suggest that the flap domain encodes the docking motif for phosphorylated Rabs. Consistent with this hypothesis, a PPM1J chimaera with the PPM1H flap domain dephosphorylates pThr72 of Rab8a both in vitro and in cellular assays. Therefore, PPM1H has acquired a Rab-specific interaction domain within a conserved phosphatase fold.   FILE DECRIPTIONS Figure 1D Rab8A.tif: Scans of Coomassie stained gels shown in Fig.1D: Left: Coomassie stained Phos-tag gel of PPM1H with Rab8A Right: Coomassie stained Phos-tag gel of PPM1J with Rab8A Figure 1D Rab10.tif: Scans of Coomassie stained gels shown in Fig.1D: Upper gel: Coomassie stained Phos-tag gel of PPM1H with Rab10 Lower gel: Coomassie stained Phos-tag gel of PPM1J with Rab10 Figure 2A gel.tif: Coomassie-stained SDS-PAGE gel showing the result of crosslinking of PPM1H D288A with phospho-Rab8A. Figure 2BC. List of cross-links with distances.xlsx: List of crosslinks identified between PPM1H D288A with phospho-Rab8A shown in Fig.2B and Fig.2C. In green crosslinks ≤32 Å, in red crosslinks >32 Å, in grey crosslinks mapping to the flexible loops missing from the crystal structure. Figure 2DEF Malachite.xlsx: Numerical data for the charts shown in Fig.2D, Fig.2E and Fig.2F. Figure 3B-WT.afe7 Astra data file with data shown in Fig.3B (left) Figure 3B-2Glu.afe7 Astra data file with data shown in Fig.3B (right) Figure 3C gel.tif: Coomassie stained gel of recombinant PPM1H WT and mutant proteins shown in Fig.3C Figure 3D Malachite.xlsx: Numerical data for the charts shown in Fig.3D Figure 4A - sequences of the chimaeras.txt: Aminoacid sequences of the chimaeric proteins used in the assays Figure 4B.tif: Coomassie stained gel of recombinant PPM phosphatases shown in Fig.4B. Last lane containing phosphatase PPM1A not shown in figure. Figure 4CD Malachite.xlsx: Numerical data for the charts shown in Fig.4C and Fig.4D. Figure 4E 700.tif: Top to bottom: <ol> <li>Total LRRK2 blot shown in Fig.4E</li> <li>HA blot for PPM phosphatases (PPM constructs) shown In Fig.4E</li> <li>GAPDH loading controls for blots in Fig.4E</li> <li>HA blot for Rab8A shown in Fig.4E</li> </ol> Figure 4E 800.tif: <ol> <li>Phospho-Rab8A Thr72 blot shown in Fig.4E</li> </ol> Figure 4F 700.tif: Top to bottom: <ol> <li>Total LRRK2 blot shown in Fig.4F</li> <li>HA blot for PPM phosphatases (PPM constructs). HA blot was not used for Fig.4F. Membrane was reblotted, shown in tif file Figure 4F 700-2</li> <li>GAPDH loading controls for blots in Fig.4F</li> <li>HA blot for Rab10. HA blot was not used for Fig.4F. Membrane was reblotted, shown in tif file Figure 4F 700-2</li> </ol> Figure 4F 700-2.tif: Top to bottom: <ol> <li>HA blot for PPM phosphatases (PPM constructs) shown In Fig.4F</li> <li>GAPDH loading controls for blots in Fig.4F</li> <li>HA blot for Rab10 shown in Fig.4F</li> </ol> Figure 4F 800.tif: <ol> <li>Phospho-Rab10 Thr73 blot shown in Fig.4F</li> </ol> Figure 5BE Malachite.xlsx: Numerical data for the charts shown in Fig.5B and Fig.5E. Figure 5C.tif: Coomassie stained gel of recombinant PPM1H WT and mutant proteins shown in Fig.5C Figure 5D 700.png: Top to bottom: <ol> <li>Total LRRK2 blot shown in Fig.5D</li> <li>HA blot for PPM phosphatases (PPM constructs) shown in Fig.5D</li> <li>GAPDH loading control for blots in Fig.5D</li> <li>HA blot for Rab10 shown in Fig.5D</li> </ol> Figure 5D 800.png: Phospho-Rab10 pThr73 blot shown in Fig.5D Figure 5E.tif: Coomassie stained gel of recombinant PPM1H WT and mutant proteins shown in Fig.5E Figure 5F 700 Rab8A.png: Top to bottom (Rab8A) <ol> <li>Total LRRK2 blot shown in Fig.5F</li> <li>HA blot for PPM phosphatases (PPM constructs) shown in Fig.5F</li> <li>GAPDH loading control for blots in Fig.5F</li> <li>HA blot for Rab8A shown in Fig.5F</li> </ol> Figure 5F 800 Rab8A.png: Phospho-Rab8A pThr72 blot shown in Fig.5F Figure 5F 700 Rab10.png: Top to bottom (Rab10) <ol> <li>Total LRRK2 blot shown in Fig.5F</li> <li>HA blot for PPM phosphatases (PPM constructs) shown in Fig.5F</li> <li>GAPDH loading control for blots in Fig.5F</li> <li>HA blot for Rab10 shown in Fig.5F</li> </ol> Figure 5F 800 Rab10.png: Phospho-Rab10 pThr73 blot shown in Fig.5F Figure 6B 700.tif: Top to bottom: <ol> <li>Total LRRK2 blot shown in Fig.6B</li> <li>HA blot for PPM phosphatases (PPM constructs) shown In Fig.6B</li> <li>GAPDH loading controls for blots in Fig.6B</li> <li>HA blot for Rab10 shown in Fig.6B</li> </ol> Figure 6B 800.tif: <ol> <li>Phospho-Rab10 Thr73 blot shown in Fig.6B</li> </ol> Figure EV1A 700.tif: Top to bottom: <ol> <li>Total LRRK2 blot shown in Fig.EV1A</li> <li>GAPDH loading controls for blots in Fig.EV1A</li> <li>HA blot for Rab10 shown in Fig.EV1A</li> </ol> Figure EV1A 800.tif: <ol> <li>HA blot for PPM phosphatases (PPM constructs) shown In Fig.EV1A</li> <li>Phospho-Rab10 Thr72 blot shown in Fig.EV1A</li> </ol> Figure EV1B.tif: Scans of Coomassie stained gels shown in Fig.EV1B Figure EV2C Malachite.xlsx: Numerical data for the chart shown in Fig.EV2C

opencc-by-4.0Jun 2021View details →

dryad36/100

Symbiotic nitrogen fixation does not stimulate soil phosphatase activity under temperate and tropical trees

Symbiotic nitrogen (N)-fixing plants can enrich ecosystems with N, which can alter the cycling and demand for other nutrients. Researchers have hypothesized that fixed N could be used by plants and soil microbes to produce extracellular phosphatase enzymes, which release P from organic matter. Consistent with this speculation, the presence of N-fixing plants is often associated with high phosphatase activity, either in the soil or on root surfaces, although other studies have not found this association, and the connection between phosphatase and rates of N fixation—the mechanistic part of the argument—is tenuous. Here, we measured soil phosphatase activity under N-fixing trees and non-fixing trees transplanted and grown in tropical and temperate sites in the USA: two sites in Hawaii, and one each in New York and Oregon. This provides a rare example of phosphatase activity measured in a multi-site field experiment with rigorously quantified rates of N fixation. We found no difference in soil phosphatase activity under N-fixing vs. non-fixing trees nor across rates of N fixation, though we note that no sites were P limited and only one was N limited. Our results add to the literature showing no connection between N fixation rates and phosphatase activity.

opencc-zeroFeb 2023View details →

dryad36/100

Data for: Potential of root acid phosphatase activity to reduce phosphorus fertilization in maize cultivated in Brazil

Potential of root acid phosphatase activity to reduce phosphorus fertilization in maize cultivated in Brazil It is urgent to mitigate the environmental impacts resulting from agriculture, especially in highly biodiverse and threatened areas, as the Brazilian Cerrado. We aim to investigate whether root acid phosphatase activity is an alternative plant strategy for nutrient acquisition in maize genotypes cultivated under fertilized and unfertilized conditions in Brazil, potentially contributing to reducing the use of phosphate fertilizers needed for production. Three experiments were performed: the first was conducted in a glasshouse, with 17 experimental maize inbred lines and two phosphorus (P) treatments; the second in the field, with three maize inbred lines and two treatments, one without fertilization and another with NPK fertilization; and the third was also carried out in the field, with 13 commercial hybrids, grown either under NK or under NPK treatment. Plant variables were measured and tested for the response to fertilization, differences amongst genotypes and response to root acid phosphatase activity. The activity of root acid phosphatase was modulated by the availability of P and nitrogen (N) in the soil and promoted grain filling of commercial hybrids in soils with low P availability. These results demonstrate that it is possible to select genotypes that are more adapted to low soil P availability aiming at organic production or to use genotypes that have high phosphatase activity under P fertilization to reduce the amount of added P needed for maize production in Brazil.

opencc-zeroOct 2023View details →

ClinicalTrials.gov36/100

(Revival) Study to Investigate the Efficacy and Safety of Alkaline Phosphatase in Patients With Sepsis-Associated AKI

ClinicalTrials.gov study NCT04411472. IPD Sharing: Not stated. Countries: 15. Publications: 2.

restrictedIPD-UNDECIDEDFeb 2026View details →

ClinicalTrials.gov36/100

Two-Arm Study of a DNA Vaccine Encoding Prostatic Acid Phosphatase (PAP) in Patients With Non-Metastatic Castrate-Resistant Prostate Cancer

ClinicalTrials.gov study NCT00849121. IPD Sharing: Not stated. Countries: 1. Publications: 1.

restrictedIPD-UNDECIDEDFeb 2026View details →

dryad36/100