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172 results on '"Serysheva, Irina I"'

5. Disrupted Ca2+ homeostasis and immunodeficiency in patients with functional IP3 receptor subtype 3 defects

Author

Neumann, Julika, Van Nieuwenhove, Erika, Terry, Lara E., Staels, Frederik, Knebel, Taylor R., Welkenhuyzen, Kirsten, Ahmadzadeh, Kourosh, Baker, Mariah R., Gerbaux, Margaux, Willemsen, Mathijs, Barber, John S., Serysheva, Irina I., De Waele, Liesbeth, Vermeulen, François, Schlenner, Susan, Meyts, Isabelle, Yule, David I., Bultynck, Geert, Schrijvers, Rik, Humblet-Baron, Stephanie, and Liston, Adrian

Published
2023
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7. Author Correction: Disrupted Ca2+ homeostasis and immunodeficiency in patients with functional IP3 receptor subtype 3 defects

Author

Neumann, Julika, Van Nieuwenhove, Erika, Terry, Lara E., Staels, Frederik, Knebel, Taylor R., Welkenhuyzen, Kirsten, Ahmadzadeh, Kourosh, Baker, Mariah R., Gerbaux, Margaux, Willemsen, Mathijs, Barber, John S., Serysheva, Irina I., De Waele, Liesbeth, Vermeulen, François, Schlenner, Susan, Meyts, Isabelle, Yule, David I., Bultynck, Geert, Schrijvers, Rik, Humblet-Baron, Stephanie, and Liston, Adrian

Published
2023
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9. Structural Insights into IP3R Function

Author

Serysheva, Irina I., Baker, Mariah R., Fan, Guizhen, COHEN, IRUN R., Series Editor, LAJTHA, ABEL, Series Editor, LAMBRIS, JOHN D., Series Editor, PAOLETTI, RODOLFO, Series Editor, REZAEI, NIMA, Series Editor, and Krebs, Joachim, editor

Published
2017
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13. Author Correction: Disrupted Ca2+ homeostasis and immunodeficiency in patients with functional IP3 receptor subtype 3 defects

Author

Neumann, Julika, primary, Van Nieuwenhove, Erika, additional, Terry, Lara E., additional, Staels, Frederik, additional, Knebel, Taylor R., additional, Welkenhuyzen, Kirsten, additional, Ahmadzadeh, Kourosh, additional, Baker, Mariah R., additional, Gerbaux, Margaux, additional, Willemsen, Mathijs, additional, Barber, John S., additional, Serysheva, Irina I., additional, De Waele, Liesbeth, additional, Vermeulen, François, additional, Schlenner, Susan, additional, Meyts, Isabelle, additional, Yule, David I., additional, Bultynck, Geert, additional, Schrijvers, Rik, additional, Humblet-Baron, Stephanie, additional, and Liston, Adrian, additional

Published
2022
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14. Disrupted Ca2+ homeostasis and immunodeficiency in patients with functional IP3 receptor subtype 3 defects

Author

Neumann, Julika, primary, Van Nieuwenhove, Erika, additional, Terry, Lara E., additional, Staels, Frederik, additional, Knebel, Taylor R., additional, Welkenhuyzen, Kirsten, additional, Ahmadzadeh, Kourosh, additional, Baker, Mariah R., additional, Gerbaux, Margaux, additional, Willemsen, Mathijs, additional, Barber, John S., additional, Serysheva, Irina I., additional, De Waele, Liesbeth, additional, Vermeulen, François, additional, Schlenner, Susan, additional, Meyts, Isabelle, additional, Yule, David I., additional, Bultynck, Geert, additional, Schrijvers, Rik, additional, Humblet-Baron, Stephanie, additional, and Liston, Adrian, additional

Published
2022
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16. Functional determination of calcium-binding sites required for the activation of inositol 1,4,5-trisphosphate receptors

Author

Arige, Vikas, Terry, Lara E., Wagner, Larry E., Malik, Sundeep, Baker, Mariah R., Fan, Guizhen, Joseph, Suresh K., Serysheva, Irina I, Yule, David I., Arige, Vikas, Terry, Lara E., Wagner, Larry E., Malik, Sundeep, Baker, Mariah R., Fan, Guizhen, Joseph, Suresh K., Serysheva, Irina I, and Yule, David I.

Abstract

Inositol 1,4,5-trisphosphate receptors (IP3Rs) initiate a diverse array of physiological responses by carefully orchestrating intracellular calcium (Ca2+) signals in response to various external cues. Notably, IP3R channel activity is determined by several obligatory factors, including IP3, Ca2+, and ATP. The critical basic amino acid residues in the N-terminal IP3-binding core (IBC) region that facilitate IP3 binding are well characterized. In contrast, the residues conferring regulation by Ca2+ have yet to be ascertained. Using comparative structural analysis of Ca2+-binding sites identified in two main families of intracellular Ca2+-release channels, ryanodine receptors (RyRs) and IP3Rs, we identified putative acidic residues coordinating Ca2+ in the cytosolic calcium sensor region in IP3Rs. We determined the consequences of substituting putative Ca2+ binding, acidic residues in IP3R family members. We show that the agonist-induced Ca2+ release, single-channel open probability (P0), and Ca2+ sensitivities are markedly altered when the negative charge on the conserved acidic side chain residues is neutralized. Remarkably, neutralizing the negatively charged side chain on two of the residues individually in the putative Ca2+-binding pocket shifted the Ca2+ required to activate IP3R to higher concentrations, indicating that these residues likely are a component of the Ca2+ activation site in IP3R. Taken together, our findings indicate that Ca2+ binding to a well-conserved activation site is a common underlying mechanism resulting in increased channel activity shared by IP3Rs and RyRs.

Published
2022

19. In situ structure of the AcrAB-TolC efflux pump at subnanometer resolution

Author

Chen, Muyuan, Shi, Xiaodong, Yu, Zhili, Fan, Guizhen, Serysheva, Irina I, Baker, Matthew L, Luisi, Ben F, Ludtke, Steven J, Wang, Zhao, Luisi, Ben [0000-0003-1144-9877], and Apollo - University of Cambridge Repository

Subjects
Models, Molecular, Electron Microscope Tomography, AcrAB-TolC, Protein Conformation, Escherichia coli Proteins, Lipoproteins, Cryoelectron Microscopy, in situ, Membrane Transport Proteins, biochemical phenomena, metabolism, and nutrition, Ligands, cryo-ET, Allosteric Regulation, subnanometer resolution, Escherichia coli, bacteria, multidrug efflux pump, Multidrug Resistance-Associated Proteins, Carrier Proteins, Bacterial Outer Membrane Proteins
Abstract

The tripartite AcrAB-TolC assembly, which spans both the inner and outer membranes in Gram-negative bacteria, is an efflux pump that contributes to multidrug resistance. Here, we present the in situ structure of full-length Escherichia coli AcrAB-TolC determined at 7 Å resolution by electron cryo-tomography. The TolC channel penetrates the outer membrane bilayer through to the outer leaflet and exhibits two different configurations that differ by a 60° rotation relative to the AcrB position in the pump assembly. AcrA protomers interact directly with the inner membrane and with AcrB via an interface located in proximity to the AcrB ligand-binding pocket. Our structural analysis suggests that these AcrA-bridged interactions underlie an allosteric mechanism for transmitting drug-evoked signals from AcrB to the TolC channel within the pump. Our study demonstrates the power of in situ electron cryo-tomography, which permits critical insights into the function of bacterial efflux pumps.

Published
2022

23. Disrupted Ca2+ homeostasis and immunodeficiency in patients with functional Inositol 1,4,5-trisphosphate receptor subtype 3 defects

Author

Neumann, Julika, primary, Van Nieuwenhove, Erika, additional, Terry, Lara E, additional, Staels, Frederik, additional, Knebel, Taylor R, additional, Welkenhuyzen, Kirsten, additional, Baker, Mariah R, additional, Gerbaux, Margaux, additional, Willemsen, Mathijs, additional, Barber, John S., additional, Serysheva, Irina I, additional, De Waele, Liesbeth, additional, Vermeulen, François, additional, Meyts, Isabelle, additional, Yule, David I, additional, Bultynck, Geert, additional, Schrijvers, Rik, additional, Humblet-Baron, Stephanie, additional, and Liston, Adrian, additional

Published
2021
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26. The skeletal muscle [Ca.sup.2+] release channel has an oxidoreductase-like domain

Author

Baker, Matthew L., Serysheva, Irina I., Sencer, Serap, Wu, Yili, Ludtke, Steven J., Jiang, Wen, Hamilton, Susan L., and Chiu, Wah

Subjects
Striated muscle -- Physiological aspects, Calcium channels -- Physiological aspects, Muscle proteins -- Physiological aspects, Structure-activity relationships (Biochemistry) -- Analysis, Science and technology
Abstract

We used a combination of bioinformatics, electron cryomicroscopy, and biochemical techniques to identify an oxidoreductase-like domain in the skeletal muscle [Ca.sup.2+] release channel protein (RyR1). The initial prediction was derived from sequence-based fold recognition for the N-terminal region (41-420) of RyR1. The putative domain was computationally localized to the clamp domain in the cytoplasmic region of a 22[Angstrom] structure of RyR1. This localization was subsequently confirmed by difference imaging with a sequence specific antibody. Consistent with the prediction of an oxidoreductase domain, RyR1 binds [[sup.3]H]NA[D.sup.+], supporting a model in which RyR1 has a oxidoreductase-like domain that could function as a type of redox sensor.

Published
2002

34. An allosteric transport mechanism for the AcrAB-TolC multidrug efflux pump

Author

Wang, Zhao, Fan, Guizhen, Hryc, Corey F, Blaza, James N, Serysheva, Irina I, Schmid, Michael F, Chiu, Wah, Luisi, Ben F, Du, Dijun, Luisi, Ben [0000-0003-1144-9877], Du, Dijun [0000-0002-1546-8939], and Apollo - University of Cambridge Repository

Subjects
AcrZ, TolC, Protein Conformation, QH301-705.5, Science, education, Allosteric Regulation, biophysics, Escherichia coli, carb, structural biology, Biology (General), Escherichia coli Proteins, Cryoelectron Microscopy, E. coli, biochemical phenomena, metabolism, and nutrition, AcrA, Biophysics and Structural Biology, Anti-Bacterial Agents, drug efflux, tripartite assembly, Medicine, Carrier Proteins, Research Article
Abstract

Bacterial efflux pumps confer multidrug resistance by transporting diverse antibiotics from the cell. In Gram-negative bacteria, some of these pumps form multi-protein assemblies that span the cell envelope. Here, we report the near-atomic resolution cryoEM structures of the Escherichia coli AcrAB-TolC multidrug efflux pump in resting and drug transport states, revealing a quaternary structural switch that allosterically couples and synchronizes initial ligand binding with channel opening. Within the transport-activated state, the channel remains open even though the pump cycles through three distinct conformations. Collectively, our data provide a dynamic mechanism for the assembly and operation of the AcrAB-TolC pump. DOI: http://dx.doi.org/10.7554/eLife.24905.001

Published
2017

39. Single-Particle Cryo-EM of the Ryanodine Receptor Channel in an Aqueous Environment

Author

Baker, Mariah R., Fan, Guizhen, and Serysheva, Irina I.

Subjects
Ryanodine receptor, Membrane proteins, Detergents, Reviews, Electron cryo-microscopy, Cryospecimen preparation, Amphipol
Abstract

Ryanodine receptors (RyRs) are tetrameric ligand-gated Ca(2+) release channels that are responsible for the increase of cytosolic Ca(2+) concentration leading to muscle contraction. Our current understanding of RyR channel gating and regulation is greatly limited due to the lack of a high-resolution structure of the channel protein. The enormous size and unwieldy shape of Ca(2+) release channels make X-ray or NMR methods difficult to apply for high-resolution structural analysis of the full-length functional channel. Single-particle electron cryo-microscopy (cryo-EM) is one of the only effective techniques for the study of such a large integral membrane protein and its molecular interactions. Despite recent developments in cryo-EM technologies and break-through single-particle cryo-EM studies of ion channels, cryospecimen preparation, particularly the presence of detergent in the buffer, remains the main impediment to obtaining atomic-resolution structures of ion channels and a multitude of other integral membrane protein complexes. In this review we will discuss properties of several detergents that have been successfully utilized in cryo-EM studies of ion channels and the emergence of the detergent alternative amphipol to stabilize ion channels for structure-function characterization. Future structural studies of challenging specimen like ion channels are likely to be facilitated by cryo-EM amenable detergents or alternative surfactants.

Published
2015

40. Inositol 1,4,5-trisphosphate receptor type 1 autoantibodies in paraneoplastic and non-paraneoplastic peripheral neuropathy

Author

Jarius, Sven, primary, Ringelstein, Marius, additional, Haas, Jürgen, additional, Serysheva, Irina I., additional, Komorowski, Lars, additional, Fechner, Kai, additional, Wandinger, Klaus-Peter, additional, Albrecht, Philipp, additional, Hefter, Harald, additional, Moser, Andreas, additional, Neuen-Jacob, Eva, additional, Hartung, Hans-Peter, additional, Wildemann, Brigitte, additional, and Aktas, Orhan, additional

Published
2016
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