The mitotic spindle mediates inheritance of the Golgi ribbon structure

Wei, Jen Hsuan; Seemann, Joachim

doi:10.1083/jcb.200809090

Cited by 49 publications

(67 citation statements)

References 24 publications

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“…Specific isoforms of these kinases, MEK1b and ERK1c have also been found to reside in the Golgi and regulate its fragmentation during mitosis (16,17). These studies point to the role of the MEK/ERK pathway in remodeling the Golgi structure in response to mitogen signaling (42).…”

Section: Discussionmentioning

confidence: 83%

Tethering Function of the Caspase Cleavage Fragment of Golgi Protein p115 Promotes Apoptosis via a p53-dependent Pathway

How

Shields

2011

Journal of Biological Chemistry

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The Golgi apparatus undergoes extensive fragmentation during apoptosis due in part to caspase-mediated cleavage of its structural proteins. Significantly, the Golgi-vesicle-tethering protein p115 is cleaved at Asp 757 early during apoptosis and the nuclear translocation of its 205 amino acid C-terminal fragment (CTF) precedes observable Golgi fragmentation. Nuclear localization of the p115 CTF induces apoptosis. The regulation of CTF nuclear translocation and the mechanism of its apoptotic activity however, remain unknown. Here, we demonstrate that nuclear translocation of the CTF is regulated by SUMOylation. CTF-induced apoptosis is transcription dependent and mediated by the tumor suppressor, p53. Expression of the CTF led to the phosphorylation and stabilization of p53 and results in the expression of PUMA, a pro-apoptotic target of p53. CTF-induced stabilization of p53 is sensitive to the MEK/ERK inhibitor U0126. Co-immunoprecipitation studies indicate that the p115 CTF can bind to both p53 and ERK1. The CTF is also able to form dimers and its dimerization is dependent on residues 859 -884, previously determined to be required for apoptosis. Indeed, CTF expression promotes p53-ERK interaction, which is diminished upon deletion of residues 859 -884. Together, our results indicate a conserved tethering function of the Golgi protein p115 CTF which promotes p53-ERK interaction for the amplification of the apoptotic signal.

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Section: Discussionmentioning

confidence: 83%

Tethering Function of the Caspase Cleavage Fragment of Golgi Protein p115 Promotes Apoptosis via a p53-dependent Pathway

How

Shields

2011

Journal of Biological Chemistry

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“…These events are most likely reversed as the organelle reforms during mitotic exit (Fig. 6) (Gaietta et al, 2006;Miller et al, 2009;Wei and Seemann, 2009) in a process that may also involve centrosome motility (Piel et al, 2001).…”

Section: Discussionmentioning

confidence: 99%

“…One mechanism for organelle partitioning is transformation into vesicles that are dispersed throughout the cytoplasm. However, organelle inheritance is not only a stochastic process, but shares similarity with the ordered segregation of chromosomes that depends on the microtubule (MT)-based mitotic spindle (Shima et al, 1998;Jokitalo et al, 2001;Shorter and Warren, 2002;Wei and Seemann, 2009). Thus, breakdown of the NE does not involve vesiculation, but transfer of its components to the ER in a process that is linked to spindle formation (Ellenberg et al, 1997;Burke and Ellenberg, 2002;Puhka et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

Division of the intermediate compartment at the onset of mitosis provides a mechanism for Golgi inheritance

Marie

Dale

Kouprina

et al. 2012

Journal of Cell Science

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SummaryAs mammalian cells prepare for mitosis, the Golgi ribbon is first unlinked into its constituent stacks and then transformed into spindleassociated, pleiomorphic membrane clusters in a process that remains enigmatic. Also, it remains unclear whether Golgi inheritance involves the incorporation of Golgi enzymes into a pool of coat protein I (COPI) vesicles, or their COPI-independent transfer to the endoplasmic reticulum (ER). Based on the observation that the intermediate compartment (IC) at the ER-Golgi boundary is connected to the centrosome, we examined its mitotic fate and possible role in Golgi breakdown. The use of multiple imaging techniques and markers revealed that the IC elements persist during the M phase, maintain their compositional and structural properties and remain associated with the mitotic spindle, forming circular arrays at the spindle poles. At G2/M transition, the movement of the pericentrosomal domain of the IC (pcIC) to the cell centre and its expansion coincide with the unlinking of the Golgi ribbon. At prophase, coupled to centrosome separation, the pcIC divides together with recycling endosomes, providing novel landmarks for mitotic entry. We provide evidence that the permanent IC elements function as way stations during the COPI-dependent dispersal of Golgi components at prometa-and metaphase, indicating that they correspond to the previously described Golgi clusters. In addition, they continue to communicate with the vesicular 'Golgi haze' and thus are likely to provide templates for Golgi reassembly. These results implicate the IC in mitotic Golgi inheritance, resulting in a model that integrates key features of the two previously proposed pathways.

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“…In mammalian cultured cells, the Golgi ribbon is fragmented into smaller pieces by the onset of mitosis (Rabouille and Jolo, 2003;Shima et al, 1998). Wei and Seemann reported that COPI vesicles accumulate around the centrosomes prior to anaphase initiation (Wei and Seemann, 2009). Moreover, the vesicles are transferred by the mitotic spindles during mitosis.…”

Section: Dependence Of Copi Vesicle Distribution On Astral Microtubulmentioning

confidence: 99%

COPI-mediated membrane trafficking is required for cytokinesis inDrosophilamale meiotic divisions

Kitazawa

Yamaguchi

Mori

et al. 2012

Journal of Cell Science

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SummaryThe coatomer protein complex, COPI, mediates retrograde vesicle transport from the Golgi apparatus to the ER. Here, we investigated the meiotic phenotype of Drosophila melanogaster spermatocytes expressing dsRNA of 52 genes encoding membrane-traffickingrelated factors. We identified COPI as an essential factor for male meiosis. In Drosophila male meiotic divisions, COPI is localized in the ER-Golgi intermediate compartment of tER-Golgi units scattered throughout the spermatocyte cytoplasm. Prior to chromosome segregation, the vesicles assemble at the spindle pole periphery through a poleward movement, mediated by minus-end motor dynein along astral microtubules. At the end of each meiotic division, COPI-containing vesicles are equally partitioned between two daughter cells. Our present data strongly suggest that spermatocytes possess a regulatory mechanism for equal inheritance of several types of membrane vesicles. Using testis-specific knockdown of COPI subunits or the small GTPase Arf or mutations of the cCOP gene, we examined the role of COPI in male meiosis. COPI depletion resulted in the failure of cytokinesis, through disrupted accumulation of essential proteins and lipid components at the cleavage furrow region. Furthermore, it caused a reduction in the number of overlapping central spindle microtubules, which are essential for cytokinesis. Drosophila spermatocytes construct ER-based intracellular structures associated with astral and spindle microtubules. COPI depletion resulted in severe disruption of these ER-based structures. Thus, we propose that COPI plays an important role in Drosophila male meiosis, not only through vesicle transport to the cleavage furrow region, but also through the formation of ER-based structures.

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The mitotic spindle mediates inheritance of the Golgi ribbon structure

Cited by 49 publications

References 24 publications

Tethering Function of the Caspase Cleavage Fragment of Golgi Protein p115 Promotes Apoptosis via a p53-dependent Pathway

Tethering Function of the Caspase Cleavage Fragment of Golgi Protein p115 Promotes Apoptosis via a p53-dependent Pathway

Division of the intermediate compartment at the onset of mitosis provides a mechanism for Golgi inheritance

COPI-mediated membrane trafficking is required for cytokinesis inDrosophilamale meiotic divisions

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