Abstract / Description of output
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 language | English |
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Pages (from-to) | 2777-85 |
Number of pages | 9 |
Journal | Journal of Cell Science |
Volume | 124 |
Issue number | Pt 16 |
DOIs | |
Publication status | Published - 15 Aug 2011 |
Keywords / Materials (for Non-textual outputs)
- 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