State of the APC/C: Organization, function, and structure

McLean, Janel R.; Chaix, Denis; Ohi, Melanie D.; Gould, Kathleen L.

doi:10.3109/10409238.2010.541420

Cited by 59 publications

(90 citation statements)

References 260 publications

(431 reference statements)

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“…Although the APC/C plays an important regulatory role in the eukaryotic cell cycle and has been subject to numerous studies (12), still much has to be learned on its biochemical structure and regulation. For example, only recently, APC16 had been identified as a functional APC/C component in animals (33,34) and, similarly, UVI4 and UVI4-like/OSD1/GIG1 as plant-specific inhibitors of APC/C (22,23).…”

Section: Discussionmentioning

confidence: 99%

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SAMBA, a plant-specific anaphase-promoting complex/cyclosome regulator is involved in early development and A-type cyclin stabilization

Eloy

González

Leene

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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The anaphase-promoting complex/cyclosome (APC/C) is a large multiprotein E3 ubiquitin ligase involved in ubiquitin-dependent proteolysis of key cell cycle regulatory proteins, including the destruction of mitotic cyclins at the metaphase-to-anaphase transition. Despite its importance, the role of the APC/C in plant cells and the regulation of its activity during cell division remain poorly understood. Here, we describe the identification of a plant-specific negative regulator of the APC/C complex, designated SAMBA. In Arabidopsis thaliana, SAMBA is expressed during embryogenesis and early plant development and plays a key role in organ size control. Samba mutants produced larger seeds, leaves, and roots, which resulted from enlarged root and shoot apical meristems, and, additionally, they had a reduced fertility attributable to a hampered male gametogenesis. Inactivation of SAMBA stabilized A2-type cyclins during early development. Our data suggest that SAMBA regulates cell proliferation during early development by targeting CYCLIN A2 for APC/C-mediated proteolysis.

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Section: Discussionmentioning

confidence: 99%

“…One of the most complex ubiquitin ligases involved in cell cycle control is the anaphase-promoting complex/cyclosome (APC/C), of which the composition can vary from 11 to 13 subunits depending on the organism. The APC/C complex plays essential roles in mitosis, meiosis, and postmitotically differentiated cells (3,(9)(10)(11)(12).…”

mentioning

confidence: 99%

SAMBA, a plant-specific anaphase-promoting complex/cyclosome regulator is involved in early development and A-type cyclin stabilization

Eloy

González

Leene

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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“…APC/C: APC/C is perhaps the most complex ubiquitin ligase. Its core is composed of 13 subunits (Apc1, Apc2, Cdc27, Apc4, Apc5, Cdc16, Cdc23, Apc9, Doc1, Apc11, Cdc26, Swm1, and Mnd2), with Apc11 being the RING domain component that binds Ubc1 and Ubc4, the two primary E2s functioning with yeast APC/C (McLean et al 2011). The core APC/C associates with one of three activators that bind substrates and are crucial targets for APC/C regulation.…”

Section: Ring Domain Ubiquitin Ligasesmentioning

confidence: 99%

The Ubiquitin–Proteasome System of Saccharomyces cerevisiae

et al. 2012

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Protein modifications provide cells with exquisite temporal and spatial control of protein function. Ubiquitin is among the most important modifiers, serving both to target hundreds of proteins for rapid degradation by the proteasome, and as a dynamic signaling agent that regulates the function of covalently bound proteins. The diverse effects of ubiquitylation reflect the assembly of structurally distinct ubiquitin chains on target proteins. The resulting ubiquitin code is interpreted by an extensive family of ubiquitin receptors. Here we review the components of this regulatory network and its effects throughout the cell.

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“…The APC/C is an E3 ubiquitin ligase made up of multiple proteins, which requires an activator for proper substrate selection (reviewed in McLean et al 2011). During meiosis, the Cdc20 mitotic activator is required along with Ama1 to regulate APC/C activity (Pesin and Orr-Weaver 2008;Cooper and Strich 2011).…”

mentioning

confidence: 99%

Timely Closure of the Prospore Membrane Requires SPS1 and SPO77 in Saccharomyces cerevisiae

et al. 2016

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During sporulation in Saccharomyces cerevisiae, a double lipid bilayer called the prospore membrane is formed de novo, growing around each meiotic nucleus and ultimately closing to create four new cells within the mother cell. Here we show that SPS1, which encodes a kinase belonging to the germinal center kinase III family, is involved in prospore membrane development and is required for prospore membrane closure. We find that SPS1 genetically interacts with SPO77 and see that loss of either gene disrupts prospore membrane closure in a similar fashion. Specifically, cells lacking SPS1 and SPO77 produce hyperelongated prospore membranes from which the leading edge protein complex is not removed from the prospore membrane in a timely fashion. The SPS1/ SPO77 pathway is required for the proper phosphorylation and stability of Ssp1, a member of the leading edge protein complex that is removed and degraded when the prospore membrane closes. Genetic dissection of prospore membrane closure finds SPS1 and SPO77 act in parallel to a previously described pathway of prospore membrane closure that involves AMA1, an activator of the meiotic anaphase promoting complex.KEYWORDS prospore membrane; meiotic exit; anaphase promoting complex; sporulation; cytokinesis; germinal center kinase B IOLOGICAL membranes provide a barrier for inhibiting the flow of materials between a cell and its surroundings and for compartmentalizing the contents of the various organelles within a cell. The size and shape of membranes are central to their functions. Membranes are essential for many fundamental cellular processes including ion balance, energy generation, and secretion. In cell division, membrane dynamics are particularly important, where they act to segregate the contents of the cellular progeny.The process of cell division differs among cells. Most commonly, animal cells divide through a mechanism requiring the assembly of an actin-based contractile ring at the division site (reviewed in Green et al. 2012). This actomyosin ring contracts and matures, ultimately leading to scission of the membrane necks mediated by the ESCRTIII (endosomal sorting complex required for transport III) complex. However, other variations of cytokinesis occur: cellularization during early Drosophila embryogenesis, which requires the growth of membranes around the nuclei before the contractile event (Lee and Harris 2014) and cell division in plants, which requires the secretion of vesicles to the division plane to form the phragmoplast, which will eventually separate the two daughter cells (reviewed in Jürgens 2005). Actin is not always involved in cytokinesis; although prokaryotic cells have actin-like filaments (reviewed in Carballido-López 2006), these filaments are not used for cytokinesis (Pollard and Wu 2010). Similarly, cytokinesis in Trypanosoma brucei (a bikont eukaryote) does not require actin but seems to utilize microtubules (Wheeler et al. 2013). In the budding yeast Saccharomyces cerevisiae, an actin-based contractile ring plays a role in ...

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State of the APC/C: Organization, function, and structure

Cited by 59 publications

References 260 publications

SAMBA, a plant-specific anaphase-promoting complex/cyclosome regulator is involved in early development and A-type cyclin stabilization

SAMBA, a plant-specific anaphase-promoting complex/cyclosome regulator is involved in early development and A-type cyclin stabilization

The Ubiquitin–Proteasome System of Saccharomyces cerevisiae

Timely Closure of the Prospore Membrane Requires SPS1 and SPO77 in Saccharomyces cerevisiae

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