MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QG, UK.
J Cell Sci. 2011 Aug 15;124(Pt 16):2777-85. doi: 10.1242/jcs.084319.
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.
pacsin（也称为 syndapin）蛋白家族在结构上具有很好的特征。它们包含与膜曲率的产生或维持相关的 F-BAR 结构域。这些蛋白质的细胞生物学功能仍不太清楚。在这里，我们最初证实，EHD2 是一种先前在小窝（caveolae）部分被证明存在于小窝部分并与 pacsin 结合的蛋白质，是一种小窝蛋白。我们接着报道 GFP-pacsin 2 可以被招募到小窝中，并且内源性 pacsin 2 部分与质膜上的 caveolin 1 共定位。使用小干扰 RNA（siRNA）分析 pacsin 2 在小窝生物发生中的作用表明，pacsin 2 功能的丧失导致形态定义的小窝丧失和 caveolin 蛋白在质膜内的积累。pacsin 2 的 F-BAR 结构域（而不是相关的 CIP4 和 FBP17 的 F-BAR 结构域）的过表达会破坏小窝的形态发生或运输，这意味着 pacsin 2 与这些过程所需的成分相互作用。我们提出 pacsin 2 在质膜小窝的形成中具有重要作用。
