P-selectin glycoprotein ligand-1 (PSGL-1), a glycoprotein expressed on the cell surface of leukocytes, binds to selectins and mediates leukocyte rolling on the vascular endothelium. Here we report that PSGL-1 binds to the C-terminal (G3 domain) of the extracellular proteoglycan PG-M/versican. Cells transfected with PSGL-1 or a shorter form containing the binding site, or cells expressing endogenous PSGL-1 aggregate in the presence of versican or G3 product. The aggregation appears to be induced by G3 multimers that bind to PSGL-1 and form a network. Endogenous versican and/or G3-containing fragments also bind to PSGL-1 in human plasma. Removal of the endogenous G3-containing fragments reduces the effect of plasma on leukocyte aggregation. Finally, the roles of G3-containing fragments in leukocyte aggregation were confirmed in a mouse model. Taken together, our results strongly support a physiologically relevant role for PSGL-1/versican binding and may have implications in the immunoresponse.
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Special Issue – Cell Biology of Mitochondria
Our special issue on ‘Cell Biology of Mitochondria’ is now complete. Explore this issue and read the Editorial from our Guest Editors Ana J. García-Sáez and Heidi McBride.
Save the date – Imaging Cell Dynamics
We are delighted to announce that we will be hosting a 2026 Imaging Cell Dynamics meeting. This meeting will provide a unique opportunity to bring together experts working at the interface between cell biology and imaging. Save the date for 11-14 May 2026 and register for more information.
Origin and evolution of mitochondrial inner membrane composition
In this Review, Kailash Venkatraman and colleagues provide an examination of the morphological similarities between prokaryotic intracytoplasmic membranes and mitochondrial inner membranes, and whether cristae evolution has driven specialisation of the mitochondrial lipidome.
Resolution in super-resolution microscopy
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