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Phosphorylation of Bok at Ser-8 blocks its ability to suppress IPR-mediated calcium mobilization.
Cell Commun Signal
January 2025
Department of Pharmacology, SUNY Upstate Medical University, Syracuse, NY, 13210, USA.
Background: Bok is a poorly characterized Bcl-2 protein family member with roles yet to be clearly defined. It is clear, however, that Bok binds strongly to inositol 1,4,5-trisphosphate (IP) receptors (IPRs), which govern the mobilization of Ca from the endoplasmic reticulum, a signaling pathway required for many cellular processes. Also known is that Bok has a highly conserved phosphorylation site for cAMP-dependent protein kinase at serine-8 (Ser-8).
View Article and Find Full Text PDFA reduction-secretion system contributes to roxarsone (V) degradation and efflux in Brevundimonas sp. M20.
BMC Microbiol
January 2025
School of Laboratory Animal & Shandong Laboratory Animal Center, Shandong First Medical University, Shandong Academy of Medical Sciences, Ji'nan, Shandong, 250117, China.
Roxarsone (V) (Rox(V)) is an organoarsenical compound that poses significant risks to aquatic ecosystems and various diseases. Reducing trivalent 3-amino-4-hydroxyphenylarsonic acid (HAPA(III)) offers a competitive advantage; however, it leads to localized arsenic contamination, which can disrupt the soil microbiome and impede plant growth. Three genes, BsntrA, arsC2, and BsexpA, encoding nitroreductase, arsenate reductase, and MFS transporter, respectively, were identified in the Rox(V)-resistant strain Brevundimonas sp.
View Article and Find Full Text PDFStructure of transmembrane AMPA receptor regulatory protein subunit γ2.
Nat Commun
January 2025
Solomon H. Snyder Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Transmembrane AMPA receptor regulatory proteins (TARPs) are claudin-like proteins that tightly regulate AMPA receptors (AMPARs) and are fundamental for excitatory neurotransmission. With cryo-electron microscopy (cryo-EM) we reconstruct the 36 kDa TARP subunit γ2 to 2.3 Å, which points to structural diversity among TARPs.
View Article and Find Full Text PDFAdiponectin removal by the human kidney: A preliminary study.
Nutr Metab Cardiovasc Dis
November 2024
Department of Internal Medicine, Genoa University, Italy.
Background And Aims: The adipocyte-derived adiponectin (APN) has potent insulin-sensitizing and anti-inflammatory properties. The adipose tissue is known to be the main source for APN in the circulation, but sites and mechanisms which remove APN from blood are still unknown in humans.
Methods And Results: We reviewed APN data obtained in previous studies in which the inter-organ exchange of amino acids and cytokines was measured in our laboratory.
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