Help Privacy Policy Disclaimer
  Advanced SearchBrowse




Journal Article

delta-COP contains a helix C-terminal to its longin domain key to COPI dynamics and function.

There are no MPG-Authors in the publication available
External Resource
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)

(Supplementary material), 3MB


Arakel, E. C., Richter, K. P., Clancy, A., & Schwappach, B. (2016). delta-COP contains a helix C-terminal to its longin domain key to COPI dynamics and function. Proceedings of the National Academy of Sciences of the United States of America, 113(25), 6916-6921. doi:10.1073/pnas.1603544113.

Cite as: https://hdl.handle.net/11858/00-001M-0000-002A-F5CD-E
Membrane recruitment of coatomer and formation of coat protein I (COPI)-coated vesicles is crucial to homeostasis in the early secretory pathway. The conformational dynamics of COPI during cargo capture and vesicle formation is incompletely understood. By scanning the length of delta-COP via functional complementation in yeast, we dissect the domains of the delta-COP subunit. We show that the mu-homology domain is dispensable for COPI function in the early secretory pathway, whereas the N-terminal longin domain is essential. We map a previously uncharacterized helix, C-terminal to the longin domain, that is specifically required for the retrieval of HDEL-bearing endoplasmic reticulum-luminal residents. It is positionally analogous to an unstructured linker that becomes helical and membrane-facing in the open form of the AP2 clathrin adaptor complex. Based on the amphipathic nature of the critical helix it may probe the membrane for lipid packing defects or mediate interaction with cargo and thus contribute to stabilizing membrane-associated coatomer.