Specificity of the anaphase Biology Diagrams The anaphase-promoting complex/cyclosome (APC/C) is an E3 cullin-RING ligase that mediates ubiquitin-dependent proteolysis of specific regulatory proteins to control chromosome segregation in mitosis, the events of cytokinesis and mitotic exit, maintenance of G1, and the initiation of DNA replication 2,3. Through its cullin-RING catalytic
The anaphase-promoting complex or cyclosome (APC/C) is an unusually large multi-subunit cullin-RING E3 ubiquitin ligase that functions to regulate progression through, and exit from, the mitotic phase of the cell cycle and controls entry into the S phase ([1
Molecule of the Month: Anaphase Biology Diagrams
The anaphase promoting complex/cyclosome (APC/C) is a ubiquitin ligase that has essential functions in and outside the eukaryotic cell cycle. It is the most complex molecular machine that is known 1. The anaphase promoting complex or cyclosome regulates cell cycle transitions. The anaphase promoting complex or cyclosome (APC/C) is a multi-subunit cullin-RING E3 ubiquitin ligase that functions to regulate progression through the mitotic phase of the cell cycle and to control entry into S phase [1-4].The APC/C also plays a role in regulating meiosis, and has been implicated in post Anaphase-promoting complex / cyclosome (APC/C) is a central gatekeeper of the cell cycle. Although its name suggests that it promotes "anaphase" - a specific step in the cell cycle - APC/C is a large protein complex that monitors many stages of the cell cycle. It helps in removing regulatory proteins, allowing cells to move from one step to
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 and RING subunit much like SCF. Other parts The anaphase-promoting complex/cyclosome (APC/C) is a large E3 ligase that mediates ubiquitin-dependent proteolysis of cell cycle regulatory proteins to control various events during replication In mitosis, the activation of a large ubiquitin-protein ligase, the anaphase-promoting complex (APC), is required for anaphase initiation and for exit from mitosis. We show that APC is under complex control by a network of regulatory factors, CDC20, CDH1 and MAD2. CDC20 and CDH1 are activators of APC; they bind directly to APC and activate its
Molecular architecture and mechanism of the anaphase Biology Diagrams
Key events in mitosis such as sister chromatid separation and subsequent inactivation of cyclin-dependent kinase 1 are regulated by ubiquitin-dependent proteolysis. These events are mediated by the anaphase-promoting complex (APC), a cell cycle-regulated ubiquitin ligase that assembles multiubiquitin chains on regulatory proteins such as securin and cyclins and thereby targets them for
