Relevant bibliographies by topics / Microdomain compartmentalization

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'Microdomain compartmentalization'

Author: Grafiati
Published: 11 March 2023
Last updated: 31 July 2025

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Journal articles on the topic "Microdomain compartmentalization"

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Sobolczyk, Marta, and Tomasz Boczek. "ROLE OF MEMBRANE MICRODOMAIN COMPARTMENTALIZATION IN GABA-MEDIATED SIGNAL TRANSDUCTION." IBRO Neuroscience Reports 15 (October 2023): S259. http://dx.doi.org/10.1016/j.ibneur.2023.08.443.

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Watson, Robert T., Satoshi Shigematsu, Shian-Huey Chiang, et al. "Lipid raft microdomain compartmentalization of TC10 is required for insulin signaling and GLUT4 translocation." Journal of Cell Biology 154, no. 4 (2001): 829–40. http://dx.doi.org/10.1083/jcb.200102078.

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Recent studies indicate that insulin stimulation of glucose transporter (GLUT)4 translocation requires at least two distinct insulin receptor–mediated signals: one leading to the activation of phosphatidylinositol 3 (PI-3) kinase and the other to the activation of the small GTP binding protein TC10. We now demonstrate that TC10 is processed through the secretory membrane trafficking system and localizes to caveolin-enriched lipid raft microdomains. Although insulin activated the wild-type TC10 protein and a TC10/H-Ras chimera that were targeted to lipid raft microdomains, it was unable to acti
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Terrin, Anna, Stefania Monterisi, Alessandra Stangherlin, et al. "PKA and PDE4D3 anchoring to AKAP9 provides distinct regulation of cAMP signals at the centrosome." Journal of Cell Biology 198, no. 4 (2012): 607–21. http://dx.doi.org/10.1083/jcb.201201059.

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Previous work has shown that the protein kinase A (PKA)–regulated phosphodiesterase (PDE) 4D3 binds to A kinase–anchoring proteins (AKAPs). One such protein, AKAP9, localizes to the centrosome. In this paper, we investigate whether a PKA–PDE4D3–AKAP9 complex can generate spatial compartmentalization of cyclic adenosine monophosphate (cAMP) signaling at the centrosome. Real-time imaging of fluorescence resonance energy transfer reporters shows that centrosomal PDE4D3 modulated a dynamic microdomain within which cAMP concentration selectively changed over the cell cycle. AKAP9-anchored, centroso
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Collin, Guillaume, Mélanie Franco, Valérie Simon, Christine Bénistant, and Serge Roche. "The Tom1L1-Clathrin Heavy Chain Complex Regulates Membrane Partitioning of the Tyrosine Kinase Src Required for Mitogenic and Transforming Activities." Molecular and Cellular Biology 27, no. 21 (2007): 7631–40. http://dx.doi.org/10.1128/mcb.00543-07.

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ABSTRACT Compartmentalization of Src tyrosine kinases (SFK) plays an important role in signal transduction induced by a number of extracellular stimuli. For example, Src mitogenic signaling induced by platelet-derived growth factor (PDGF) is initiated in cholesterol-enriched microdomain caveolae. How this Src subcellular localization is regulated is largely unknown. Here we show that the Tom1L1-clathrin heavy chain (CHC) complex negatively regulates the level of SFK in caveolae needed for the induction of DNA synthesis. Tom1L1 is both an interactor and a substrate of SFK. Intriguingly, it stim
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Hong, Dihui, Dov Jaron, Donald G. Buerk, and Kenneth A. Barbee. "Transport-dependent calcium signaling in spatially segregated cellular caveolar domains." American Journal of Physiology-Cell Physiology 294, no. 3 (2008): C856—C866. http://dx.doi.org/10.1152/ajpcell.00278.2007.

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We developed a two-dimensional model of transport-dependent intracellular calcium signaling in endothelial cells (ECs). Our purpose was to evaluate the effects of spatial colocalization of endothelial nitric oxide synthase (eNOS) and capacitative calcium entry (CCE) channels in caveolae on eNOS activation in response to ATP. Caveolae are specialized microdomains of the plasma membrane that contain a variety of signaling molecules to optimize their interactions and regulate their activity. In ECs, these molecules include CCE channels and eNOS. To achieve a quantitative understanding of the mech
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Frolikova, Michaela, Eliska Valaskova, Jiri Cerny, et al. "Addressing the Compartmentalization of Specific Integrin Heterodimers in Mouse Sperm." International Journal of Molecular Sciences 20, no. 5 (2019): 1004. http://dx.doi.org/10.3390/ijms20051004.

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Integrins are transmembrane cell receptors involved in two crucial mechanisms for successful fertilization, namely, mammalian intracellular signaling and cell adhesion. Integrins α6β4, α3β1 and α6β1 are three major laminin receptors expressed on the surface of mammalian cells including gametes, and the presence of individual integrin subunits α3, α6, β1 and β4 has been previously detected in mammalian sperm. However, to date, proof of the existence of individual heterodimer pairs in sperm and their detailed localization is missing. The major conclusion of this study is evidence that the β4 int
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Aota, Hiroyuki, Yotaro Morishima, and Mikiharu Kamachi. "COMPARTMENTALIZATION OF ZINQII) TETRAPHENYLPORPHYRIN IN A HYDROPHOBIC MICRODOMAIN OF AN AMPHIPHILIC POLYELECTROLYTE: A PHYSICOCHEMICAL MODEL OF BIOLOGICAL METALLOPORPHYRIN SYSTEMS." Photochemistry and Photobiology 57, s1 (1993): 989–95. http://dx.doi.org/10.1111/j.1751-1097.1993.tb02960.x.

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Marchetti, Marta, Marie-Noelle Monier, Alexandre Fradagrada, et al. "Stat-mediated Signaling Induced by Type I and Type II Interferons (IFNs) Is Differentially Controlled through Lipid Microdomain Association and Clathrin-dependent Endocytosis of IFN Receptors." Molecular Biology of the Cell 17, no. 7 (2006): 2896–909. http://dx.doi.org/10.1091/mbc.e06-01-0076.

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Type I (α/β) and type II (γ) interferons (IFNs) bind to distinct receptors, although they activate the same signal transducer and activator of transcription, Stat1, raising the question of how signal specificity is maintained. Here, we have characterized the sorting of IFN receptors (IFN-Rs) at the plasma membrane and the role it plays in IFN-dependent signaling and biological activities. We show that both IFN-α and IFN-γ receptors are internalized by a classical clathrin- and dynamin-dependent endocytic pathway. Although inhibition of clathrin-dependent endocytosis blocked the uptake of IFN-α
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Bavari, Sina, Catharine M. Bosio, Elizabeth Wiegand, et al. "Lipid Raft Microdomains." Journal of Experimental Medicine 195, no. 5 (2002): 593–602. http://dx.doi.org/10.1084/jem.20011500.

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Spatiotemporal aspects of filovirus entry and release are poorly understood. Lipid rafts act as functional platforms for multiple cellular signaling and trafficking processes. Here, we report the compartmentalization of Ebola and Marburg viral proteins within lipid rafts during viral assembly and budding. Filoviruses released from infected cells incorporated raft-associated molecules, suggesting that viral exit occurs at the rafts. Ectopic expression of Ebola matrix protein and glycoprotein supported raft-dependent release of filamentous, virus-like particles (VLPs), strikingly similar to live
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Grisan, Francesca, Liliana F. Iannucci, Nicoletta C. Surdo, et al. "PKA compartmentalization links cAMP signaling and autophagy." Cell Death & Differentiation 28, no. 8 (2021): 2436–49. http://dx.doi.org/10.1038/s41418-021-00761-8.

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AbstractAutophagy is a highly regulated degradative process crucial for maintaining cell homeostasis. This important catabolic mechanism can be nonspecific, but usually occurs with fine spatial selectivity (compartmentalization), engaging only specific subcellular sites. While the molecular machines driving autophagy are well understood, the involvement of localized signaling events in this process is not well defined. Among the pathways that regulate autophagy, the cyclic AMP (cAMP)/protein kinase A (PKA) cascade can be compartmentalized in distinct functional units called microdomains. Howev
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Dissertations / Theses on the topic "Microdomain compartmentalization"

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Balycheva, Marina. "Microdomain–specific localization of functional L-type calcium channels in atrial cardiomyocytes: novel concept of local regulation and remodelling in disease." Doctoral thesis, 2015. http://hdl.handle.net/11562/924530.

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no<br>Recently, novel concept of microdomain-specific regulation in cardiac cells have greatly extended our understanding of how specific subcellular localization impacts on channel function and regulation. Microdomain is a small region of cell membrane, which has a distinct structure, composition and function. It has been recognized that discrete clusters of different ion channels exist in the sarcolemma in different microdomains such as T-tubules, caveolae. This study addresses the hypothesis that distinct spatial compartmentalization of functional calcium channels in different intercell
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Book chapters on the topic "Microdomain compartmentalization"

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Redden, John M., Kimberly L. Dodge-Kafka, and Michael S. Kapiloff. "Function to Failure: Compartmentalization of Cardiomyocyte Signaling by A-Kinase-Anchoring Proteins." In Microdomains in the Cardiovascular System. Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-54579-0_3.

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Conference papers on the topic "Microdomain compartmentalization"

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Mayer, Jonathan, Yutong Wang, Anna I. Neel, Haiguo Sun, and Rong Chen. "Cholesterol Enrichment Alters Compartmentalization of G-Proteins Into Lipid Raft Microdomains." In ASPET 2024 Annual Meeting Abstract. American Society for Pharmacology and Experimental Therapeutics, 2024. http://dx.doi.org/10.1124/jpet.141.130365.

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Journal articles
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