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Pacsin 2 is recruited to caveolae and functions in caveolar biogenesis

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Original languageEnglish
Pages (from-to)2777-85
Number of pages9
JournalJournal of Cell Science
Issue numberPt 16
Publication statusPublished - 15 Aug 2011


The pacsin (also termed syndapin) protein family is well characterised structurally. They contain F-BAR domains associated with the generation or maintenance of membrane curvature. The cell biology of these proteins remains less understood. Here, we initially confirm that EHD2, a protein previously shown biochemically to be present in caveolar fractions and to bind to pacsins, is a caveolar protein. We go on to report that GFP-pacsin 2 can be recruited to caveolae, and that endogenous pacsin 2 partially colocalises with caveolin 1 at the plasma membrane. Analysis of the role of pacsin 2 in caveolar biogenesis using small interfering RNA (siRNA) reveals that loss of pacsin 2 function results in loss of morphologically defined caveolae and accumulation of caveolin proteins within the plasma membrane. Overexpression of the F-BAR domain of pacsin 2 (but not the related F-BAR domains of CIP4 and FBP17) disrupts caveolar morphogenesis or trafficking, implying that pacsin 2 interacts with components required for these processes. We propose that pacsin 2 has an important role in the formation of plasma membrane caveolae.

    Research areas

  • Adaptor Proteins, Signal Transducing, Animals, Carrier Proteins, Caveolae, Caveolin 1, Cell Membrane, Cloning, Molecular, Fibroblasts, Humans, Mice, Microscopy, Electron, NIH 3T3 Cells, Protein Structure, Tertiary, Protein Transport, Proteins, RNA, Small Interfering, Transgenes

ID: 24502062