Taxonomic distribution of proteins containing APC10 domains

The tree below includes only several representative species and genera. The complete taxonomic breakdown of all proteins containing APC10 domains can be accessed here. Click the counts or percentage values to display the corresponding proteins.

Activity of the APC(Cdh1) form of the anaphase-promoting complex persists until Sphase and prevents the premature expression of Cdc20p.

Huang JN, Park I, Ellingson E, Littlepage LE, Pellman D
J Cell Biol. 2001; 154: 85-94

Cell cycle progression is driven by waves of cyclin expression coupled withregulated protein degradation. An essential step for initiating mitosis is theinactivation of proteolysis mediated by the anaphase-promoting complex/cyclosome (APC/C) bound to its regulator Cdh1p/Hct1p. Yeast APC(Cdh1) was proposedpreviously to be inactivated at Start by G1 cyclin/cyclin-dependent kinase (CDK).Here, we demonstrate that in a normal cell cycle APC(Cdh1) is inactivated in agraded manner and is not extinguished until S phase. Complete inactivation ofAPC(Cdh1) requires S phase cyclins. Further, persistent APC(Cdh1) activitythroughout G1 helps to ensure the proper timing of Cdc20p expression. Thissuggests that S phase cyclins have an important role in allowing the accumulationof mitotic cyclins and further suggests a regulatory loop among S phase cyclins, APC(Cdh1), and APC(Cdc20).

Characterization of the DOC1/APC10 subunit of the yeast and the humananaphase-promoting complex.

Grossberger R, Gieffers C, Zachariae W, Podtelejnikov AV, Schleiffer A, Nasmyth K, Mann M, Peters JM
J Biol Chem. 1999; 274: 14500-7

The anaphase-promoting complex/cyclosome (APC) is a ubiquitin-protein ligasewhose activity is essential for progression through mitosis. The vertebrate APCis thought to be composed of 8 subunits, whereas in budding yeast severaladditional APC-associated proteins have been identified, including a 33-kDaprotein called Doc1 or Apc10. Here, we show that Doc1/Apc10 is a subunit of theyeast APC throughout the cell cycle. Mutation of Doc1/Apc10 inactivates the APCwithout destabilizing the complex. An ortholog of Doc1/Apc10, which we callAPC10, is associated with the APC in different vertebrates, including humans and frogs. Biochemical fractionation experiments and mass spectrometric analysis of acomponent of the purified human APC show that APC10 is a genuine APC subunitwhose cellular levels or association with the APC are not cell cycle-regulated.We have further identified an APC10 homology region, which we propose to call theDOC domain, in several protein sequences that also contain either cullin or HECT domains. Cullins are present in several ubiquitination complexes including theAPC, whereas HECT domains represent the catalytic core of a different type ofubiquitin-protein ligase. DOC domains may therefore be important for reactionscatalyzed by several types of ubiquitin-protein ligases.