Pacsin 2 is recruited to caveolae and functions in caveolar biogenesis

Carsten Gram Hansen, Gillian Howard, Benjamin J Nichols

Research output: Contribution to journalArticlepeer-review


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.

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


  • 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


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