The S. pombe cdc15 gene is a key element in the reorganization of F-actin at mitosis

Fankhauser, Christian; Reymond, Alexandre; Cerutti, Lorenzo; Utzig, Suzan; Hofmann, Kay; Simanis, Viesturs

doi:10.1016/0092-8674(95)90432-8

Cited by 242 publications

(336 citation statements)

References 36 publications

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“…Taken together, our data favor the model that Cdc15p could promote tER biogenesis at the division site. It has been shown that overexpression of Cdc15p causes actin relocalization to the equatorial region in interphase cells (Fankhauser et al, 1995). To assess whether this is sufficient for the early secretory pathway compartments polarization, we overexpressed Cdc15p under the nmt1 promoter in cells arrested in interphase by the use of cdc25-22 genetic background (Gould and Nurse, 1989).…”

Section: Early Secretory Pathway In Fission Yeastmentioning

confidence: 99%

“…During early mitosis, actin is assembled into a ring structure through the action of several actin nucleating and bundling proteins and molecular motors. These include the formin Cdc12p (Chang et al, 1997), profilin Cdc3p (Balasubramanian et al, 1992), the extended Fer/CIP4 (EFC) domain protein Cdc15p (Fankhauser et al, 1995), and the myosin heavy chain Myo2p (Kitayama et al, 1997) together with its light chains Cdc4p (McCollum et al, 1995;Naqvi et al, 1999) and Rlc1p (Le Goff et al, 2000). It has been proposed that activation of the signaling cascade referred to as the septation initiation network (SIN) triggers actomyosin ring constriction upon nuclear division (for review see Krapp et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

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The Actomyosin Ring Recruits Early Secretory Compartments to the Division Site in Fission Yeast

Vještica

Tang

Oliferenko

2008

MBoC

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The ultimate goal of cytokinesis is to establish a membrane barrier between daughter cells. The fission yeast Schizosaccharomyces pombe utilizes an actomyosin-based division ring that is thought to provide physical force for the plasma membrane invagination. Ring constriction occurs concomitantly with the assembly of a division septum that is eventually cleaved. Membrane trafficking events such as targeting of secretory vesicles to the division site require a functional actomyosin ring suggesting that it serves as a spatial landmark. However, the extent of polarization of the secretion apparatus to the division site is presently unknown. We performed a survey of dynamics of several fluorophore-tagged proteins that served as markers for various compartments of the secretory pathway. These included markers for the endoplasmic reticulum, the COPII sites, and the early and late Golgi. The secretion machinery exhibited a marked polarization to the division site. Specifically, we observed an enrichment of the transitional endoplasmic reticulum (tER) accompanied by Golgi cisternae biogenesis. These processes required actomyosin ring assembly and the function of the EFC-domain protein Cdc15p. Cdc15p overexpression was sufficient to induce tER polarization in interphase. Thus, fission yeast polarizes its entire secretory machinery to the cell division site by utilizing molecular cues provided by the actomyosin ring. INTRODUCTIONCell division is the final event in the cell cycle that results in physical separation of two daughter cells. Despite being studied for more than a hundred years, the underlying molecular mechanisms and the cytological details of the process are still emerging. Various organisms and cell types have established multiple pathways to conduct cell division that are regulated at both signaling and structural levels (for review see Balasubramanian et al., 2004). In recent years, the fission yeast Schizosaccharomyces pombe has emerged as an attractive model for the study of cytokinesis because of its fully sequenced genome (Wood et al., 2002), a cell size convenient for cytological studies and the availability of a large set of conditional mutants compromised in various aspects of cell division (Chang et al., 1996;Balasubramanian et al., 1998).On entry into mitosis, S. pombe assembles an actomyosin ring that is thought to drive a binary cell fission through constriction, similar to many other eukaryotes, including nematodes, insects, and vertebrates (for review see Hales et al., 1999). During early mitosis, actin is assembled into a ring structure through the action of several actin nucleating and bundling proteins and molecular motors. These include the formin Cdc12p (Chang et al., 1997), profilin Cdc3p (Balasubramanian et al., 1992), the extended Fer/CIP4 (EFC) domain protein Cdc15p (Fankhauser et al., 1995), and the myosin heavy chain Myo2p (Kitayama et al., 1997) together with its light chains Cdc4p (McCollum et al., 1995;Naqvi et al., 1999) and Rlc1p (Le Goff et al., 2000). It has been proposed tha...

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Section: Early Secretory Pathway In Fission Yeastmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The Actomyosin Ring Recruits Early Secretory Compartments to the Division Site in Fission Yeast

Vještica

Tang

Oliferenko

2008

MBoC

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“…In particular, the regulation of budding yeast Hof1p appears to be conserved between SIN and MEN. Fission yeast Cdc15p is one of two functional homologues of Hof1p [51][52][53], which is the only established target of budding yeast Mob1p/ Dbf2p in cytokinesis [37]. Furthermore, Cdc15p is phosphorylated on a conserved RXXS motif that can be targeted by Mob1p/Sid2p [53].…”

Section: Septation Initiation Network (Sin) In Schizosaccharomyces Pombementioning

confidence: 99%

Hippo signalling in the G2/M cell cycle phase: Lessons learned from the yeast MEN and SIN pathways

Hergovich

Hemmings

2012

Seminars in Cell & Developmental Biology

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Over the past decade Hippo kinase signalling has been established as an essential tumour suppressor pathway controlling tissue growth in flies and mammals. All members of the Hippo core signalling cassette are conserved from yeast to humans, whereby the yeast analogues of Hippo, Mats and Lats are central components of the mitotic exit network and septation initiation network in budding and fission yeast, respectively. Here, we discuss how far core Hippo signalling components in Drosophila melanogaster and mammals have reported similar mitotic functions as already established for their highly conserved yeast counterparts.

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“…PSTPIP appears to be the mammalian homologue of the fission yeast Schizosaccharomyces pombe CDC15p, a protein involved in the organization of the cytokinetic cleavage furrow (20). It was reported that PSTPIP associates with cortical actin during most of the cell cycle and translocates at the cleavage furrow during cytokinesis (18).…”

mentioning

confidence: 99%

PSTPIP Is a Substrate of PTP-PEST and Serves as a Scaffold Guiding PTP-PEST Toward a Specific Dephosphorylation of WASP

Côté¹,

Chung²,

Théberge³

et al. 2002

Journal of Biological Chemistry

116

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PSTPIP is a tyrosine-phosphorylated protein involved in the organization of the cytoskeleton. Its ectopic expression induces filipodial-like membrane extensions in NIH 3T3 cells. We previously observed a defect in cytokinesis and an increase in the tyrosine phosphorylation of PSTPIP in PTP-PEST-deficient fibroblasts. In this article, we demonstrate that PTP-PEST and PSTPIP are found in the same complexes in vivo and that they interact directly through the CTH domain of PTP-PEST and the coiled-coil domain of PSTPIP. We tested pathways that could regulate the tyrosine phosphorylation of PSTPIP. We found that the activation of the epidermal growth factor and platelet-derived growth factor receptors can induce PSTPIP phosphorylation. With the use of the PP2 inhibitor, we demonstrate that Src kinases are not involved in the epidermal growth factor-mediated phosphorylation of PSTPIP. Together with previous results, this suggests that c-Abl is the critical tyrosine kinase downstream of growth factor receptors responsible for PSTPIP phosphorylation. We also demonstrate that PTP-PEST dephosphorylates PSTPIP at tyrosine 344. Importantly, we identified tyrosine 344 as the main phosphorylation site of PSTPIP by performing tryptic phosphopeptide maps. This is an important finding since tyrosine 367 of PSTPIP was also proposed as a candidate phosphorylation site involved in the negative regulation of the association between PSTPIP and WASP. In this respect, we observed that the PSTPIP⅐ WASP complex is stable in vivo and is not affected by the phosphorylation of PSTPIP. Furthermore, we demonstrate that PSTPIP serves as a scaffold protein between PTP-PEST and WASP and allows PTP-PEST to dephosphorylate WASP. This finding suggests a possible mechanism for PTP-PEST to directly modulate actin remodeling through the PSTPIP-WASP interaction.

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The S. pombe cdc15 gene is a key element in the reorganization of F-actin at mitosis

Cited by 242 publications

References 36 publications

The Actomyosin Ring Recruits Early Secretory Compartments to the Division Site in Fission Yeast

The Actomyosin Ring Recruits Early Secretory Compartments to the Division Site in Fission Yeast

Hippo signalling in the G2/M cell cycle phase: Lessons learned from the yeast MEN and SIN pathways

PSTPIP Is a Substrate of PTP-PEST and Serves as a Scaffold Guiding PTP-PEST Toward a Specific Dephosphorylation of WASP

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