The mitotic phosphatase cdc25C at the Golgi apparatus

Noll, Andreas; Ruppenthal, Sandra; Montenarh, Mathias

doi:10.1016/j.bbrc.2006.10.142

Cited by 6 publications

(3 citation statements)

References 34 publications

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“…Indeed, similar relocation of TGN proteins to the pericentrosomal area takes place when the Golgi stacks are disassembled by BFA (Reaves and Banting, 1992; Molloy et al, 1994). This Golgi ribbon-centrosome axis could also act in the transfer of other key proteins that regulate mitotic entry, such as cyclin B2, the partner of Cdk1 (Jackman et al, 1995) and the phosphatase Cdc25C, an activator of the cyclin B2/Cdk1 complex (Noll et al, 2006). In general, the pericentrosomal accumulation of the IC elements and REs (Marie et al, 2012) could play an important role in the maturation (at G2) and separation (at prophase) of centrosomes, as well as formation of the MT-based mitotic spindle (Hehnly and Doxsey, 2014; Wei et al, 2015; Ibar and Glavic, 2017).…”

Section: Spatial Aspects Of Trafficking and Signalingmentioning

confidence: 99%

A New Look at the Functional Organization of the Golgi Ribbon

Saraste

Prydz

2019

Front. Cell Dev. Biol.

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A characteristic feature of vertebrate cells is a Golgi ribbon consisting of multiple cisternal stacks connected into a single-copy organelle next to the centrosome. Despite numerous studies, the mechanisms that link the stacks together and the functional significance of ribbon formation remain poorly understood. Nevertheless, these questions are of considerable interest, since there is increasing evidence that Golgi fragmentation – the unlinking of the stacks in the ribbon – is intimately connected not only to normal physiological processes, such as cell division and migration, but also to pathological states, including neurodegeneration and cancer. Challenging a commonly held view that ribbon architecture involves the formation of homotypic tubular bridges between the Golgi stacks, we present an alternative model, based on direct interaction between the biosynthetic (pre-Golgi) and endocytic (post-Golgi) membrane networks and their connection with the centrosome. We propose that the central domains of these permanent pre- and post-Golgi networks function together in the biogenesis and maintenance of the more transient Golgi stacks, and thereby establish “linker compartments” that dynamically join the stacks together. This model provides insight into the reversible fragmentation of the Golgi ribbon that takes place in dividing and migrating cells and its regulation along a cell surface – Golgi – centrosome axis. Moreover, it helps to understand transport pathways that either traverse or bypass the Golgi stacks and the positioning of the Golgi apparatus in differentiated neuronal, epithelial, and muscle cells.

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Section: Spatial Aspects Of Trafficking and Signalingmentioning

confidence: 99%

A New Look at the Functional Organization of the Golgi Ribbon

Saraste

Prydz

2019

Front. Cell Dev. Biol.

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“…As drug‐induced Aurora‐A inhibition generally causes a simple delay of G2/M transition (Malumbres and Perez de Castro, ), it is possible that other additional mechanisms could help to induce a potent G2‐arrest. Regarding this aspect, several key regulatory elements of the CycB/Cdk1 complex have also been found associated with the GC, including the Cdc25C phosphatase (Noll et al., ), the kinase Myt1 (Liu et al., ) and CycB2/Cdk1 complex itself (Jackman et al., ), or have been found to interact with Golgi‐associated proteins during mitosis, as demonstrated for PLK1 association with GRASP65 (Preisinger et al., ). Although the current interpretation is that these cell‐cycle related proteins are merely involved in the regulation of Golgi disassembly (Nakajima et al., ; Villeneuve et al., ), an intriguing possibility is that they could also contribute to stimulate a Golgi‐based pathway of CycB2/Cdk1 activation and regulation of mitotic entry.…”

Section: Open Questionsmentioning

confidence: 99%

Mitotic inheritance of the Golgi complex and its role in cell division

Ayala

Colanzi

2017

Biology of the Cell

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The Golgi apparatus plays essential roles in the processing and sorting of proteins and lipids, but it can also act as a signalling hub and a microtubule-nucleation centre. The Golgi complex (GC) of mammalian cells is composed of stacks connected by tubular bridges to form a continuous membranous system. In spite of this structural complexity, the GC is highly dynamic, and this feature becomes particularly evident during mitosis, when the GC undergoes a multi-step disassembly process that allows its correct partitioning and inheritance by daughter cells. Strikingly, different steps of Golgi disassembly control mitotic entry and progression, indicating that cells actively monitor Golgi integrity during cell division. Here, we summarise the basic mechanisms and the molecular players that are involved in Golgi disassembly, focussing in particular on recent studies that have revealed the fundamental signalling pathways that connect Golgi inheritance to mitotic entry and progression.

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“…The three mammalian isoforms, Cdc25A, B, and C cumulatively contribute to progression into and through mitosis by dephosphorylating the Cdk1/cyclin B complex. Recent evidence suggests these phosphatases act on distinctly localized cellular pools of Cdk substrates and other currently unidentified substrates to control the timing and distribution of mitotic activities (2, 3). Whereas mitotic progression is a cumulative effort by these phosphatases, Cdc25A is the primary regulator of the G 1 -S transition and S-phase progression via activation of Cdk2 complexes (1).…”

Section: Introductionmentioning

confidence: 99%

Multimodal Control of Cdc25A by Nitrosative Stress

Tomko

Lazo

2008

Cancer Research

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Cdc25A propels cell cycle progression, is overexpressed in numerous human cancers, and possesses oncogenic and antiapoptotic activities. Reactive oxygen species, such as hydrogen peroxide, regulate Cdc25A, but the physiologic and pathologic effects of nitric oxide ( . NO) and . NO-derived reactive species are not well defined. Herein, we report novel independent mechanisms governing Cdc25A in response to nitrosative insult. We observed direct and rapid inhibition of Cdc25A phosphatase activity after in vitro treatment with the low molecular mass cell-permeable S-nitrosothiol S-nitrosocysteine ethyl ester (SNCEE). In addition, treatment of cancer cells with SNCEE induced nitrosative stress and decreased Cdc25A protein levels in a time-dependent and concentration-dependent manner. Similarly, iNOS-derived . NO was sufficient to suppress Cdc25A expression, consistent with its role in mediating nitrosative stress. Whereas a decrease in Cdc25A half-life was not observed in response to SNCEE, we found the translational regulator eukaryotic initiation factor 2A (eIF2A) was hyperphosphorylated and total protein translation was decreased with kinetics consistent with Cdc25A loss. Inhibition of eIF2A decreased Cdc25A levels, supporting the hypothesis that SNCEE suppressed Cdc25A translation through inhibition of eIF2A. Nitrosative stress decreased the Cdc25A-bound fraction of apoptosis signal-regulating kinase-1 (ASK-1) and sensitized cells to apoptosis induced by the ASK-1-activating chemotherapeutic cis-diaminedichloroplatinum (II), suggesting that nitrosative stress-induced suppression of Cdc25A primed cells for ASK-1-dependent apoptosis. Together these data reveal novel . NO-dependent enzymatic and translational mechanisms controlling Cdc25A, and implicate Cdc25A as a mediator of . NO-dependent apoptotic signaling. [Cancer Res 2008;68(18):7457-65]

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The mitotic phosphatase cdc25C at the Golgi apparatus

Cited by 6 publications

References 34 publications

A New Look at the Functional Organization of the Golgi Ribbon

A New Look at the Functional Organization of the Golgi Ribbon

Mitotic inheritance of the Golgi complex and its role in cell division

Multimodal Control of Cdc25A by Nitrosative Stress

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