The structure of a COPII tubule

作者：O'Donnell Jason; Maddox Kerry; Stagg Scott^*

来源：Journal of Structural Biology, 2011, 173(2): 358-364.

DOI：10.1016/j.jsb.2010.09.002

• Secretory pathway
• Cryo-electron microscopy
• Cryo-electron tomography
• COPII
• Cargo
• Subvolume averaging

Nearly a third of all eukaryotic proteins are transported from the ER to the Golgi apparatus through the secretory pathway using COPII coated vesicles. Evidence suggests that this transport occurs via 500-900 angstrom vesicles that bud from the ER membrane. It has been shown that procollagen molecules utilize the COPII proteins for transport, but it is unclear how the COPII coat can accommodate these similar to 3000 angstrom long molecules. We now present a cryogenic electron tomographic reconstruction of a Sec13/31 tubule that is approximately 3300 A long containing a hollow cylindrical interior that is 300 angstrom in diameter, dimensions that are consistent with those that are required to encapsulate a procollagen molecule wrapped in a membrane and accessory COPII components. This structure suggests a novel mechanism that the COPII coat may employ to transport elongated cargo.

• 出版日期2011-2