Anaphase-promoting complex

The anaphase-promoting complex (APC) is a large protein complex containing 11–13 subunits, including a RING subunit (Apc11) and a cullin (Apc2). APC activity requires association with activator subunits (Cdc20 or Cdh1) that contribute to substrate binding.

Anaphase-promoting complex (also called the cyclosome or APC/C) is an E3 ubiquitin ligase that marks target cell cycle proteins for degradation by the 26S proteasome. The APC/C is a large complex of 11–13 subunit proteins, including a cullin (Apc2) and RING (Apc11) subunit much like SCF. Other parts of the APC/C have unknown functions but are highly conserved.[1]

It was the discovery of the APC/C (and SCF) and their key role in eukaryotic cell-cycle regulation that established the importance of ubiquitin-mediated proteolysis in cell biology. Once perceived as a system exclusively involved in removing damaged protein from the cell, ubiquitination and subsequent protein degradation by the proteasome is now perceived as a universal regulatory mechanism for signal transduction whose importance approaches that of protein phosphorylation.

In 2014, the APC/C was mapped in 3D at a resolution of less than a nanometre, which also uncovered its secondary structure. This finding could improve understanding of cancer and reveal new binding sites for future cancer drugs.[2][3]

  1. ^ Morgan DO (2007). "Chapter 3-10: The Anaphase Promoting Complex". The Cell Cycle: Principles of Control. London: New Science Press. pp. 48–49. ISBN 978-0-9539181-2-6.
  2. ^ "Scientists map one of most important proteins in life – and cancer". The Institute of Cancer Research. 20 July 2014. Retrieved 22 July 2014.
  3. ^ Chang LF, Zhang Z, Yang J, McLaughlin SH, Barford D (September 2014). "Molecular architecture and mechanism of the anaphase-promoting complex". Nature. 513 (7518): 388–393. Bibcode:2014Natur.513..388C. doi:10.1038/nature13543. PMC 4456660. PMID 25043029.