The secreted<i>Dictyostelium</i>protein CfaD is a chalone

Bakthavatsalam, Deenadayalan; Brock, Debra A.; Nikravan, N. Neda; Houston, Kevin D.; Hatton, R. Diane; Gomer, Richard H.

doi:10.1242/jcs.026682

Cited by 48 publications

(118 citation statements)

References 39 publications

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“…Cells lacking RasC (Daniel et al, 1994), the p21-activated kinase PakD (Garcia et al, 2014), Erk1 (also known as ErkA) (Gaskins et al, 1994), the Dictyostelium Akt homologs Pkba and PkgB (Meili et al, 1999(Meili et al, , 2000, and the suppressor of cAMP receptor (SCAR) component NapA (Ibarra et al, 2006) were all nonresponsive to polyphosphate-induced development (Table 3). Cells lacking the secreted factor CtnA (Brock and Gomer, 1999), the frizzled-like receptors FslB and FslK (Prabhu and Eichinger, 2006), the inositol hexakisphosphate kinase I6kA (Luo et al, 2003), the G-protein coupled receptors GrlB, GrlE and GrlH (Prabhu and Eichinger, 2006) the autocrine factor CfaD (Bakthavatsalam et al, 2008), the target of rapamycin complex 2 (TORC2) component Lst8 (Lee et al, 2005), the Dictyostelium polyphosphate kinase Ppk1 (Livermore et al, 2016), and the PTEN homolog CnrN (Tang and Gomer, 2008) did form aggregates in response to polyphosphate (Table 3). Of the transformants that were unresponsive to polyphosphate, cells lacking RasC, PakD and Erk1 were unresponsive to Mg132-induced development while cells lacking Akt (i.e.…”

Section: Proteasome Inhibition Alone Is Not Sufficient To Induce Devementioning

confidence: 99%

“…To determine whether polyphosphate might affect signaling pathways used for starvation-induced aggregation, we included previously described aggregation phenotypes for all transformants tested (Table 3) (Brock and Gomer, 1999;Luo et al, 2003;Wu and Janetopoulos, 2013;Bakthavatsalam et al, 2008;Lee et al, 2005;Livermore et al, 2016). Cells lacking both Akt homologs PkbA and PkgB, RasC or PakD have abolished aggregation in response to polyphosphate and starvation (Meili et al, 2000;Lim et al, 2001;Garcia et al, 2014), while cells lacking PkbA or NapA show delayed aggregation upon starvation but do not respond to polyphosphate-induced aggregation (Meili et al, 1999;Ibarra et al, 2006).…”

Section: Proteasome Inhibition Alone Is Not Sufficient To Induce Devementioning

confidence: 99%

“…The cells used were Dictyostelium wild-type Ax2, pakD − (DBS0350281) (Garcia et al, 2014), erk1 − (DBS0350622) (Gaskins et al, 1994), pkbA − (DBS0349876) (Meili et al, 1999), pkbA − /pkgB − (DBS0236785) (Meili et al, 2000), rasC − (DBS0236853) (Daniel et al, 1994), napA − (DBS0236596) (Ibarra et al, 2006), adrm1 − (DBS0238203) (Cherix et al, 2006), fslB − (DBS0350230) (Prabhu and Eichinger, 2006), fslK − (DBS0350229) (Prabhu and Eichinger, 2006), ctnA − (DBS0235624) (Brock and Gomer, 1999), i6kA − (DBS0236426) (Luo et al, 2003), grlB − (DBS0350074) (Prabhu and Eichinger, 2006), grlE − (DBS0350075) (Prabhu and Eichinger, 2006), grlH − (DBS0350226) (Prabhu and Eichinger, 2006), cfaD − (DBS0302444) (Bakthavatsalam et al, 2008), lst8 − (DBS0236517) (Lee et al, 2005), ppk1 − (DBS0350685) (Livermore et al, 2016) and cnrN − (DBS0302655) (Tang and Gomer, 2008). Mutant genotypes were verified by PCR, and cells were kept under constant selection.…”

Section: Dictyostelium and Human Leukemia Cell Culturementioning

confidence: 99%

“…The cell pellets were solubilized in Laemmli sample buffer containing protease and phosphatase inhibitors, and heated to 95°C for 5 min. Gel electrophoresis and blotting were performed as described previously (Bakthavatsalam et al, 2008). Blots were blocked in TBS with 4% milk and 2% BSA.…”

Section: Western Blotsmentioning

confidence: 99%

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Extracellular polyphosphate signals through Ras and Akt to prime Dictyostelium discoideum cells for development

Suess

Watson

Chen

et al. 2017

Journal of Cell Science

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Linear chains of five to hundreds of phosphates called polyphosphate are found in organisms ranging from bacteria to humans, but their function is poorly understood. In Dictyostelium discoideum, polyphosphate is used as a secreted signal that inhibits cytokinesis in an autocrine negative feedback loop. To elucidate how cells respond to this unusual signal, we undertook a proteomic analysis of cells treated with physiological levels of polyphosphate and observed that polyphosphate causes cells to decrease levels of actin cytoskeleton proteins, possibly explaining how polyphosphate inhibits cytokinesis. Polyphosphate also causes proteasome protein levels to decrease, and in both Dictyostelium and human leukemia cells, decreases proteasome activity and cell proliferation. Polyphosphate also induces Dictyostelium cells to begin development by increasing expression of the cell-cell adhesion molecule CsA (also known as CsaA) and causing aggregation, and this effect, as well as the inhibition of proteasome activity, is mediated by Ras and Akt proteins. Surprisingly, Ras and Akt do not affect the ability of polyphosphate to inhibit proliferation, suggesting that a branching pathway mediates the effects of polyphosphate, with one branch affecting proliferation, and the other branch affecting development.

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Section: Proteasome Inhibition Alone Is Not Sufficient To Induce Devementioning

confidence: 99%

Section: Proteasome Inhibition Alone Is Not Sufficient To Induce Devementioning

confidence: 99%

Section: Dictyostelium and Human Leukemia Cell Culturementioning

confidence: 99%

Section: Western Blotsmentioning

confidence: 99%

See 2 more Smart Citations

Extracellular polyphosphate signals through Ras and Akt to prime Dictyostelium discoideum cells for development

Suess

Watson

Chen

et al. 2017

Journal of Cell Science

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“…Bullough [19] coined the term "chalone" and hypothesized it as the inhibitors of cell growth through negative feedback to control the size of a tissue. A number of studies provide experimental 4 evidence in support of this hypothesis [20], [21], [22], [23].The growth in terms of the level of functionality is sensed for example, in the liver by the flux of bile acids. Bile acids are synthesized in the liver and secreted into the small intestine to facilitate digestion.…”

Section: 4mentioning

confidence: 99%

A Cell Biology Inspired Model for Managing Packet Broadcasts in Mobile Ad-hoc Networks

2015

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Abstract:This Paper proposes a packet delivery mechanism for Mobile Ad hoc Networks (MANETs) in which the nodes are not required to keep global routing information and where there are no key nodes that act as infrastructure. The solution proposed in this Paper is based on blindrebroadcasting with packet storm control through a mechanism inspired by the chalone mechanism found in biological cell divisions. The operation of the proposed protocol is mathematically modelled using cellular automata. The efficiency of the proposed protocol was compared with those of blindrebroadcasting and sequence number controlled flooding using an OMNET simulation with respect to the total number of copies of the same data packet received in the network against the number of nodes in the network. The results show a significant improvement in the performance. The protocol efficiency was also analysed with respect to the spreading of the data packet against time using an analytical model based on an epidemic model. The results show comparable performance.

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The secreted proteome profile of developing Dictyostelium discoideum cells

Bakthavatsalam

Gomer

2010

Proteomics

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Dictyostelium discoideum is a unicellular eukaryote that, when starved, aggregates to form multicellular structures. In this report, we identified the proteins secreted by developing Dictyostelium cells using mass spectrometry based proteomics. A total of 349 different secreted proteins were identified, indicating that at least 2.6% of the 13600 predicted proteins in the Dictyostelium genome are secreted. Gene ontology (GO) analysis suggests that many of the secreted proteins are involved in protein and carbohydrate metabolism, and proteolysis. KeywordsDictyostelium; development; secreted molecules; proteome Dictyostelium discoideum is a unicellular eukaryote which lives in soil and proliferates by feeding on bacteria. Upon starvation, cells stop proliferating, communicate with each other by secreting signal molecules, and aggregate to form multicellular groups [1]. Each group consists of ~ 20,000 cells that form a fruiting body, which consists of a mass of spores held up by a column of stalk cells. These spores are dispersed by the wind and germinate to amoeboid cells to continue the life cycle. Because of a wide variety of molecular biology, biochemistry, and cell biology tools to study Dictyostelium, this system is used to elucidate many different mechanisms.The Dictyostelium genome encodes 13600 predicted proteins [2,3]. Transcriptome studies have been performed to understand the complex network of signal pathways that regulate these genes and thus Dictyostelium development [4,5]. However, much remains to be understood about the proteins encoded by the genome. For instance, during development, Dictyostelium cells secrete a large number of different proteins [6], but the nature and function of most of the proteins are unknown. High-throughput identification of proteins in cells, or media conditioned by cells, can be done using mass spectrometry (MS), allowing MS-based proteomic techniques to generate proteome profiles that complement microarray data. Since many intracellular pathways are regulated by extracellular ligands, in this report we identify proteins that are secreted by developing Dictyostelium cells.To collect secreted proteins, wild-type A×2 cells were grown in shaking culture as previously described [7]. Cells at mid-log phase (3 × 10 6 cells/ml) were collected by centrifugation at 1,500 × g for 3 minutes and washed twice by resuspending the pellets in were then pipetted on to a Type 353102 1 μm pore sized polyethylene terephthalate membrane six well format cell culture insert (Becton Dickinson, Franklin Lakes, NJ). After 10 minutes, the cells had settled on, and attached to, the membrane, and the buffer was gently removed from the insert. PBM was added into the well of a six well plate, and the insert with cells was then placed in the well ( Figure 1A). The amount of buffer in the well was adjusted to just touch the membrane of the insert to keep the membrane and cells moist. The cells developed normally, with cells aggregating starting at 6 hours and forming fruiting bodies at 24 hours (...

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The secretedDictyosteliumprotein CfaD is a chalone

Cited by 48 publications

References 39 publications

Extracellular polyphosphate signals through Ras and Akt to prime Dictyostelium discoideum cells for development

Extracellular polyphosphate signals through Ras and Akt to prime Dictyostelium discoideum cells for development

A Cell Biology Inspired Model for Managing Packet Broadcasts in Mobile Ad-hoc Networks

The secreted proteome profile of developing Dictyostelium discoideum cells

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