Immunologists have long been occupied with the description of cellular activation signaling events that originate with the stimulation of multichain immunoreceptors at the cell surface. These signals are transmitted by a protein-partner-signaling cascade through the cytoplasm to the nucleus, where they culminate in changes in gene expression, metabolic state, and entry into cell cycle. For T cells and B cells, these signaling cascades start with the ligation of the T cell receptor (TCR) and B cell receptor (BCR), respectively, and result in the recruitment and activation of related families of signaling molecules at the cell surface. Until recently, this gathering of signaling proteins was thought to occur within the featureless plasma membrane, a cellular organ that was envisioned as a boundary between the inner and outer components of the cell, but which contributed little to the signaling process. However, the past few years have seen the gradual realization that activation of signaling in lymphocytes takes place in and around specialized membrane subdomains called lipid rafts (also known as DIGs and GEMs). Here, we provide a brief overview of the analogous structures and compositions of lipid raft-associated signaling complexes in T cells and B cells, and the ways in which lymphocytes--and their pathogen adversaries--use lipid rafts to their benefit.
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http://dx.doi.org/10.1126/stke.2002.122.re2 | DOI Listing |
ACS Sens
January 2025
Cancer Hospital of Dalian University of Technology, Shenyang 110042, China.
Intracellular morphological apical-basal polarity, regulated by conserved polarity proteins, plays a crucial role in cell migration and metastasis. In this study, using a genetically encoded Förster resonance energy transfer (FRET) biosensor to visually present the spatiotemporal stress state between the lipid rafts on the membrane and the linked actin, we first provide the evidence for the existence of intrinsic apical-basal stress polarity in tumor cells and demonstrate that this polarity is a prerequisite for the formation of flow-induced front-back stress polarity. Interestingly, our study revealed that the front-back stress polarity disappeared upon the disruption of intrinsic apical-basal stress discrepancy, resulting in a large attenuated cell migration activity reduced from 76.
View Article and Find Full Text PDFCell Death Dis
January 2025
Faculty of Medicine, Institute of Biochemistry I, Goethe University Frankfurt, Frankfurt, Germany.
Arachidonate 15-lipoxygenase type B (ALOX15B) peroxidises polyunsaturated fatty acids to their corresponding fatty acid hydroperoxides, which are subsequently reduced into hydroxy-fatty acids. A dysregulated abundance of these biological lipid mediators has been reported in the skin and blood of psoriatic compared to healthy individuals. RNAscope and immunohistochemistry revealed increased ALOX15B expression in lesional psoriasis samples.
View Article and Find Full Text PDFBiochim Biophys Acta Mol Basis Dis
January 2025
Department of Cell Pathology, Faculty of Biotechnology, University of Wroclaw, Wrocław, Poland. Electronic address:
The connection between the F-actin and ribosome docking to the PM has been reported, but the exact mechanism has remained unclear. Previously, we discovered that gelsolin (GSN) forms complexes with numerous ribosomal proteins, including ribosomal protein SA (RPSA). Now, we have unraveled the mechanism of ribosome recruitment to the lipid nanodomains of the PM, with GSN playing a pivotal role in this process.
View Article and Find Full Text PDFBiochim Biophys Acta Mol Cell Biol Lipids
January 2025
Budker Institute of Nuclear Physics SB RAS, Acad. Lavrentiev Ave.,9, 630090 Novosibirsk, Russia.
Terahertz (THz) radiation has gained attention due to technological advancements, but its biological effects remain unclear. We investigated the impact of 2.3 THz radiation on SK-MEL-28 cells using metabolomic and gene network analysis.
View Article and Find Full Text PDFmBio
January 2025
Division of Infectious Diseases, Boston Children's Hospital, Boston, Massachusetts, USA.
Unlabelled: Streptolysin O (SLO) is a virulence determinant of group A (), the agent of streptococcal sore throat and severe invasive infections. SLO is a member of a family of bacterial pore-forming toxins known as cholesterol-dependent cytolysins, which require cell membrane cholesterol for pore formation. While cholesterol is essential for cytolytic activity, accumulating data suggest that cell surface glycans may also participate in the binding of SLO and other cholesterol-dependent cytolysins to host cells.
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