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Yap Localization during Mechanosensing Requires Filamentous Actin [Cell Biology] (2016)

Das, A., Fischer, R. S., Pan, D., Waterman, C. M.

The American Society for Biochemistry and Molecular Biology (ASBMB)

In: Journal of Biological Chemistry

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Publication Date: 2016-03-19

Description: Cell-cell contact inhibition and the mechanical environment of cells have both been shown to regulate YAP nuclear localization to modulate cell proliferation. Changes in cellular contractility by genetic, pharmacological, and matrix stiffness perturbations regulate YAP nuclear localization. However, because contractility and F-actin organization are interconnected cytoskeletal properties, it remains unclear which of these distinctly regulates YAP localization. Here we show that in the absence of cell-cell contact, actomyosin contractility suppresses YAP phosphorylation at Ser112, however, neither loss of contractility nor increase in YAP phosphorylation is sufficient for its nuclear exclusion. We find that actin cytoskeletal integrity is essential for YAP nuclear localization, and can override phosphoregulation or contractility-mediated regulation of YAP nuclear localization. This actin-mediated regulation is conserved during mechanotransduction, as substrate compliance increased YAP phosphorylation and reduced cytoskeletal integrity leading to nuclear exclusion of both YAP and Ser(P)112-YAP. These data provide evidence for two actin-mediated pathways for YAP regulation; one in which actomyosin contractility regulates YAP phosphorylation, and a second that involves cytoskeletal integrity-mediated regulation of YAP nuclear localization independent of contractility. We suggest that in non-contact inhibited cells, this latter mechanism may be important in low stiffness regimes, such as may be encountered in physiological environments.

Print ISSN: 0021-9258

Electronic ISSN: 1083-351X

Topics: Biology , Chemistry and Pharmacology

Published by The American Society for Biochemistry and Molecular Biology (ASBMB)

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Species-specific Activation of Human TRPA1 by Protons [Neurobiology] (2013)

de la Roche, J., Eberhardt, M. J., Klinger, A. B., Stanslowsky, N., Wegner, F., Koppert, W., Reeh, P. W., Lampert, A., Fischer, M. J. M., Leffler, A.

The American Society for Biochemistry and Molecular Biology (ASBMB)

In: Journal of Biological Chemistry

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Publication Date: 2013-07-13

Description: The surveillance of acid-base homeostasis is concerted by diverse mechanisms, including an activation of sensory afferents. Proton-evoked activation of rodent sensory neurons is mainly mediated by the capsaicin receptor TRPV1 and acid-sensing ion channels. In this study, we demonstrate that extracellular acidosis activates and sensitizes the human irritant receptor TRPA1 (hTRPA1). Proton-evoked membrane currents and calcium influx through hTRPA1 occurred at physiological acidic pH values, were concentration-dependent, and were blocked by the selective TRPA1 antagonist HC030031. Both rodent and rhesus monkey TRPA1 failed to respond to extracellular acidosis, and protons even inhibited rodent TRPA1. Accordingly, mouse dorsal root ganglion neurons lacking TRPV1 only responded to protons when hTRPA1 was expressed heterologously. This species-specific activation of hTRPA1 by protons was reversed in both mouse and rhesus monkey TRPA1 by exchange of distinct residues within transmembrane domains 5 and 6. Furthermore, protons seem to interact with an extracellular interaction site to gate TRPA1 and not via a modification of intracellular N-terminal cysteines known as important interaction sites for electrophilic TRPA1 agonists. Our data suggest that hTRPA1 acts as a sensor for extracellular acidosis in human sensory neurons and should thus be taken into account as a yet unrecognized transduction molecule for proton-evoked pain and inflammation. The species specificity of this property is unique among known endogenous TRPA1 agonists, possibly indicating that evolutionary pressure enforced TRPA1 to inherit the role as an acid sensor in human sensory neurons.

Print ISSN: 0021-9258

Electronic ISSN: 1083-351X

Topics: Biology , Chemistry and Pharmacology

Published by The American Society for Biochemistry and Molecular Biology (ASBMB)

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Characterization of the CagA-CagF Interaction [Molecular Biophysics] (2013)

Bonsor, D. A., Weiss, E., Iosub-Amir, A., Reingewertz, T. H., Chen, T. W., Haas, R., Friedler, A., Fischer, W., Sundberg, E. J.

The American Society for Biochemistry and Molecular Biology (ASBMB)

In: Journal of Biological Chemistry

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Publication Date: 2013-11-16

Description: CagA is a virulence factor that Helicobacter pylori inject into gastric epithelial cells through a type IV secretion system where it can cause gastric adenocarcinoma. Translocation is dependent on the presence of secretion signals found in both the N- and C-terminal domains of CagA and an interaction with the accessory protein CagF. However, the molecular basis of this essential protein-protein interaction is not fully understood. Herein we report, using isothermal titration calorimetry, that CagA forms a 1:1 complex with a monomer of CagF with nm affinity. Peptide arrays and isothermal titration calorimetry both show that CagF binds to all five domains of CagA, each with μm affinity. More specifically, a coiled coil domain and a C-terminal helix within CagF contacts domains II-III and domain IV of CagA, respectively. In vivo complementation assays of H. pylori with a double mutant, L36A/I39A, in the coiled coil region of CagF showed a severe weakening of the CagA-CagF interaction to such an extent that it was nearly undetectable. However, it had no apparent effect on CagA translocation. Deletion of the C-terminal helix of CagF also weakened the interaction with CagA but likewise had no effect on translocation. These results indicate that the CagA-CagF interface is distributed broadly across the molecular surfaces of these two proteins to provide maximal protection of the highly labile effector protein CagA.

Print ISSN: 0021-9258

Electronic ISSN: 1083-351X

Topics: Biology , Chemistry and Pharmacology

Published by The American Society for Biochemistry and Molecular Biology (ASBMB)

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Metaphosphate Stabilization in the Myosin ATPase [Enzymology] (2013)

Kiani, F. A., Fischer, S.

The American Society for Biochemistry and Molecular Biology (ASBMB)

In: Journal of Biological Chemistry

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Publication Date: 2013-12-07

Description: It has been proposed recently that ATP hydrolysis in ATPase enzymes proceeds via an initial intermediate in which the dissociated γ-phosphate of ATP is bound in the protein as a metaphosphate (PγO3−). A combined quantum/classical analysis of this dissociated nucleotide state inside myosin provides a quantitative understanding of how the enzyme stabilizes this unusual metaphosphate. Indeed, in vacuum, the energy of the ADP3−·PγO3−·Mg2+ complex is much higher than that of the undissociated ATP4−. The protein brings it to a surprisingly low value. Energy decomposition reveals how much each interaction in the protein stabilizes the metaphosphate state; backbone peptides of the P-loop contribute 50% of the stabilization energy, and the side chain of Lys-185+ contributes 25%. This can be explained by the fact that these groups make strong favorable interactions with the α- and β-phosphates, thus favoring the charge distribution of the metaphosphate state over that of the ATP state. Further stabilization (16%) is achieved by a hydrogen bond between the backbone C=O of Ser-237 (on loop Switch-1) and a water molecule perfectly positioned to attack the PγO3− in the subsequent hydrolysis step. The planar and singly negative PγO3− is a much better target for the subsequent nucleophilic attack by a negatively charged OH− than the tetrahedral and doubly negative PγO42− group of ATP. Therefore, we argue that the present mechanism of metaphosphate stabilization is common to the large family of nucleotide-hydrolyzing enzymes. Methodologically, this work presents a computational approach that allows us to obtain a truly quantitative conception of enzymatic strategy.

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Electronic ISSN: 1083-351X

Topics: Biology , Chemistry and Pharmacology

Published by The American Society for Biochemistry and Molecular Biology (ASBMB)

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Metallocenes@COF-102: organometallic host-guest chemistry of porous crystalline organic frameworks (2011)

Suresh Babu Kalidindi; Kirill Yusenko; Roland A. Fischer

Royal Society of Chemistry (RSC)

In: Chemical Communications

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Publication Date: 2011-04-19

Description: The structure of the inclusion compound (FeCp2)4@COF-102 is dominated by [small pi]-[small pi] interactions, with a unique arrangement of FeCp2 molecules which replicates the host structure. Suresh Babu Kalidindi, Kirill Yusenko, Roland A. Fischer ( from Chem. Commun.) Suresh Babu Kalidindi, Chem. Commun., 2011, DOI: 10.1039/C1CC11450F To cite this article before page numbers are assigned, use the DOI form of citation above. The content of this RSS Feed (c) The Royal Society of Chemistry

Print ISSN: 1359-7345

Electronic ISSN: 1364-548X

Topics: Chemistry and Pharmacology

Published by Royal Society of Chemistry (RSC)

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Stepwise deposition of metal organic frameworks on flexible synthetic polymer surfaces (2011)

Mikhail Meilikhov; Kirill Yusenko; Eckhardt Schollmeyer; Christian Mayer; Hans-Jurgen Buschmann; Roland A. Fischer

Royal Society of Chemistry (RSC)

In: Dalton Transactions

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Publication Date: 2011-04-06

Description: Thin porous films of [Cu3(btc)2]n metal organic framework were deposited in a stepwise manner on surfaces of flexible organic polymers. The thickness of deposited film can be precisely controlled. The deposition of the first cycles was monitored by UV-vis spectroscopy. Mikhail Meilikhov, Kirill Yusenko, Eckhardt Schollmeyer, Christian Mayer, Hans-Jurgen Buschmann, Roland A. Fischer ( from Dalton Trans.) Mikhail Meilikhov, Dalton Trans., 2011, DOI: 10.1039/C0DT01820A To cite this article before page numbers are assigned, use the DOI form of citation above. The content of this RSS Feed (c) The Royal Society of Chemistry

Print ISSN: 1477-9226

Topics: Chemistry and Pharmacology

Published by Royal Society of Chemistry (RSC)

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Use of confocal fluorescence microscopy to compare different methods of modifying metal-organic framework (MOF) crystals with dyes (2011)

Mingyan Ma; Annika Gross Denise Zacher Antonio Pinto Heshmat Noei Yuemin Wang Roland A. Fischer Nils Metzler-Nolte

Royal Society of Chemistry (RSC)

In: CrystEngComm

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Publication Date: 2011-03-02

Description: Mingyan Ma, Annika Gross, Denise Zacher, Antonio Pinto, Heshmat Noei, Yuemin Wang, Roland A. Fischer, Nils Metzler-Nolte (Communication from CrystEngComm) Mingyan Ma, CrystEngComm, 2011, DOI: 10.1039/c0ce00416b To cite this article before page numbers are assigned, use the DOI form of citation above. The content of this RSS Feed (c) The Royal Society of Chemistry

Electronic ISSN: 1466-8033

Topics: Geosciences , Physics

Published by Royal Society of Chemistry (RSC)

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Use of confocal fluorescence microscopy to compare different methods of modifying metal-organic framework (MOF) crystals with dyes (2011)

Mingyan Ma; Annika Gross; Denise Zacher; Antonio Pinto; Heshmat Noei; Yuemin Wang; Roland A. Fischer; Nils Metzler-Nolte

Royal Society of Chemistry (RSC)

In: CrystEngComm

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Publication Date: 2011-03-29

Description: Confocal laser scanning microscopy was used to determine the distribution of fluorescent dyes adsorbed within the bulk or bonded to the external surface of MOF crystals. Mingyan Ma, Annika Gross, Denise Zacher, Antonio Pinto, Heshmat Noei, Yuemin Wang, Roland A. Fischer, Nils Metzler-Nolte ( from CrystEngComm) Mingyan Ma, CrystEngComm, 2011, DOI: 10.1039/C0CE00416B To cite this article before page numbers are assigned, use the DOI form of citation above. The content of this RSS Feed (c) The Royal Society of Chemistry

Electronic ISSN: 1466-8033

Topics: Geosciences , Physics

Published by Royal Society of Chemistry (RSC)

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MOF-on-MOF heteroepitaxy: perfectly oriented [Zn2(ndc)2(dabco)]n grown on [Cu2(ndc)2(dabco)]n thin films (2011)

O. Shekhah; K. Hirai; H. Wang; H. Uehara; M. Kondo; S. Diring; D. Zacher; R. A. Fischer; O. Sakata; S. Kitagawa; S. Furukawa; C. Woll

Royal Society of Chemistry (RSC)

In: Dalton Transactions

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Publication Date: 2011-03-29

Description: The successful heteroepitaxial growth of perfectly oriented hybrid MOF thin films was achieved by employing liquid-phase epitaxy (LPE). [Zn2(ndc)2(dabco)]n was grown on [Cu2(ndc)2(dabco)]n, thus demonstrating that the MOF-on-MOF deposition scheme developed for powdered MOF materials can also be applied in connection with LPE. O. Shekhah, K. Hirai, H. Wang, H. Uehara, M. Kondo, S. Diring, D. Zacher, R. A. Fischer, O. Sakata, S. Kitagawa, S. Furukawa, C. Woll ( from Dalton Trans.) O. Shekhah, Dalton Trans., 2011, DOI: 10.1039/C0DT01818J To cite this article before page numbers are assigned, use the DOI form of citation above. The content of this RSS Feed (c) The Royal Society of Chemistry

Print ISSN: 1477-9226

Topics: Chemistry and Pharmacology

Published by Royal Society of Chemistry (RSC)

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MOF-on-MOF heteroepitaxy: perfectly oriented [Zn2(ndc)2(dabco)]n grown on [Cu2(ndc)2(dabco)]n thin films (2011)

O. Shekhah; K. Hirai H. Wang H. Uehara M. Kondo S. Diring D. Zacher R. A. Fischer O. Sakata S. Kitagawa S. Furukawa C. Woll

Royal Society of Chemistry (RSC)

In: Dalton Transactions

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Publication Date: 2011-03-25

Description: O. Shekhah, K. Hirai, H. Wang, H. Uehara, M. Kondo, S. Diring, D. Zacher, R. A. Fischer, O. Sakata, S. Kitagawa, S. Furukawa, C. Woll (Paper from Dalton Trans.) O. Shekhah, Dalton Trans., 2011, DOI: 10.1039/c0dt01818j To cite this article before page numbers are assigned, use the DOI form of citation above. The content of this RSS Feed (c) The Royal Society of Chemistry

Print ISSN: 1477-9226

Topics: Chemistry and Pharmacology

Published by Royal Society of Chemistry (RSC)

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