scholarly journals Second messenger-mediated spatiotemporal control of protein degradation regulates bacterial cell cycle progression

2009 ◽  
Vol 23 (1) ◽  
pp. 93-104 ◽  
Author(s):  
A. Duerig ◽  
S. Abel ◽  
M. Folcher ◽  
M. Nicollier ◽  
T. Schwede ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Protein Degradation ◽  
Bacterial Cell ◽  
Cell Cycle Progression ◽  
Second Messenger ◽  
Cycle Progression ◽  
Bacterial Cell Cycle ◽  
Spatiotemporal Control

scholarly journals Untargeted metabolomics links glutathione to bacterial cell cycle progression

2020 ◽  
Vol 2 (2) ◽  
pp. 153-166 ◽  
Author(s):  
Johannes Hartl ◽  
Patrick Kiefer ◽  
Andreas Kaczmarczyk ◽  
Maximilian Mittelviefhaus ◽  
Fabian Meyer ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Bacterial Cell ◽  
Cell Cycle Progression ◽  
Untargeted Metabolomics ◽  
Cycle Progression ◽  
Bacterial Cell Cycle

Chronic Myeloid Leukemia with Variant t(9;22) Shows Dysregulated Expression of Genes Included in Pivotal Cellular Pathways

Blood ◽  
2012 ◽  
Vol 120 (21) ◽  
pp. 1674-1674
Author(s):  
Francesco Albano ◽  
Luisa Anelli ◽  
Antonella Zagaria ◽  
Nicoletta Coccaro ◽  
Luciana Impera ◽  
...  
Keyword(s):  
Gene Expression ◽  
Cell Cycle ◽  
Dna Repair ◽  
Chronic Myeloid Leukemia ◽  
Protein Degradation ◽  
Myeloid Leukemia ◽  
Cell Cycle Progression ◽  
Molecular Response ◽  
Cycle Progression ◽  
Functional Relationships

Abstract Abstract 1674 The t(9;22)(q34;q11) generating the Philadelphia chromosome and the BCR/ABL1 fusion gene represents the cytogenetic hallmark of chronic myeloid leukemia (CML). About 5–10% of CML cases show variant translocations with the involvement of other chromosomes in addition to chromosomes 9 and 22. The greater frequency of occurrence of genomic microdeletions proximally to ABL1 or distally to BCR has been reported in CML cases with variant translocations (30–40%) than in cases with a classic t(9;22) (10–18%). The prognostic significance of variant t(9;22) was unclear and debated in the pre-imatinib era, whereas recent studies of large CML series showed that the presence of variant translocations has no impact on the cytogenetic and molecular response or on prognosis (Marzocchi et al. Blood 2011,117:6793-800). However, the molecular bases of differences between CML patients with classic and variant t(9;22) have never been elucidated. Here we report a gene expression profile analysis of 8 CML cases with variant t(9;22) and 12 patients with a classic t(9;22). RNA samples were extracted from bone marrow cells and hybridized on the Agilent SurePrint G3 Human GE 8×60K Microarray slide (Agilent Technologies). Ingenuity Pathways Analysis (IPA, www.ingenuity.com) software was used to provide an accurate biological and statistical analysis of microarray experimental data revealing functional relationships among the identified genes. Gene expression analysis identified a 59 gene set able to distinguish the two CML subsets. These genes are mostly involved in the development of the hematological system and in the occurrence of hematological diseases. Forty-five out of 59 (76%) genes were up-regulated, causing the probable activation of different molecular mechanisms such as cellular responses to stimuli, protein degradation, DNA repair, cell cycle progression. IPA analysis revealed that most of the dysregulated genes are included in a network where they are functionally linked to MAPK p38, AKT, and NFKB. Moreover, several genes play a role in cytoskeleton organization (WIPF1), in signal transduction and cell cycle progression (TRIB1, PDE4B, PTK2B, PLK3), in regulation of apoptosis (ZFAND5, STK17B), and in protein degradation (ZFAND5, SNRPG). On the contrary, among the downregulated genes, 5 (BCDIN3D, TMEM68, HILPDA, TMEM68, and C17orf61) establish direct interactions with ubiquitin C (UBC), a crucial gene involved in different intracellular mechanisms such as protein degradation, DNA repair, cell cycle regulation, and the regulation of other signaling pathways. In conclusion, gene expression profiling in cases with variant t(9;22) revealed biological differences in this CML subset. Our data show an overall deregulation of genes involved in hematological system development and in cell proliferation signaling pathway. Disclosures: No relevant conflicts of interest to declare.

scholarly journals Mdm2 promotes Cdc25C protein degradation and delays cell cycle progression through the G2/M phase

Oncogene ◽  
2017 ◽  
Vol 36 (49) ◽  
pp. 6762-6773 ◽  
Author(s):  
L E Giono ◽  
L Resnick-Silverman ◽  
L A Carvajal ◽  
S St Clair ◽  
J J Manfredi
Keyword(s):  
Cell Cycle ◽  
Protein Degradation ◽  
Cell Cycle Progression ◽  
Cycle Progression ◽  
M Phase

scholarly journals A Localized Complex of Two Protein Oligomers Controls the Orientation of Cell Polarity

mBio ◽  
2017 ◽  
Vol 8 (1) ◽  
Author(s):  
Adam M. Perez ◽  
Thomas H. Mann ◽  
Keren Lasker ◽  
Daniel G. Ahrens ◽  
Michael R. Eckart ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Cell Polarity ◽  
Histidine Kinase ◽  
Bacterial Cell ◽  
Cell Cycle Progression ◽  
Caulobacter Crescentus ◽  
Cycle Progression ◽  
Self Assembling ◽  
Membrane Bound ◽  
Ordered Assembly

ABSTRACT Signaling hubs at bacterial cell poles establish cell polarity in the absence of membrane-bound compartments. In the asymmetrically dividing bacterium Caulobacter crescentus, cell polarity stems from the cell cycle-regulated localization and turnover of signaling protein complexes in these hubs, and yet the mechanisms that establish the identity of the two cell poles have not been established. Here, we recapitulate the tripartite assembly of a cell fate signaling complex that forms during the G1-S transition. Using in vivo and in vitro analyses of dynamic polar protein complex formation, we show that a polymeric cell polarity protein, SpmX, serves as a direct bridge between the PopZ polymeric network and the cell fate-directing DivJ histidine kinase. We demonstrate the direct binding between these three proteins and show that a polar microdomain spontaneously assembles when the three proteins are coexpressed heterologously in an Escherichia coli test system. The relative copy numbers of these proteins are essential for complex formation, as overexpression of SpmX in Caulobacter reorganizes the polarity of the cell, generating ectopic cell poles containing PopZ and DivJ. Hierarchical formation of higher-order SpmX oligomers nucleates new PopZ microdomain assemblies at the incipient lateral cell poles, driving localized outgrowth. By comparison to self-assembling protein networks and polar cell growth mechanisms in other bacterial species, we suggest that the cooligomeric PopZ-SpmX protein complex in Caulobacter illustrates a paradigm for coupling cell cycle progression to the controlled geometry of cell pole establishment. IMPORTANCE Lacking internal membrane-bound compartments, bacteria achieve subcellular organization by establishing self-assembling protein-based microdomains. The asymmetrically dividing bacterium Caulobacter crescentus uses one such microdomain to link cell cycle progression to morphogenesis, but the mechanism for the generation of this microdomain has remained unclear. Here, we demonstrate that the ordered assembly of this microdomain occurs via the polymeric network protein PopZ directly recruiting the polarity factor SpmX, which then recruits the histidine kinase DivJ to the developing cell pole. Further, we find that overexpression of the bridge protein SpmX in Caulobacter disrupts this ordered assembly, generating ectopic cell poles containing both PopZ and DivJ. Together, PopZ and SpmX assemble into a cooligomeric network that forms the basis for a polar microdomain that coordinates bacterial cell polarity. IMPORTANCE Lacking internal membrane-bound compartments, bacteria achieve subcellular organization by establishing self-assembling protein-based microdomains. The asymmetrically dividing bacterium Caulobacter crescentus uses one such microdomain to link cell cycle progression to morphogenesis, but the mechanism for the generation of this microdomain has remained unclear. Here, we demonstrate that the ordered assembly of this microdomain occurs via the polymeric network protein PopZ directly recruiting the polarity factor SpmX, which then recruits the histidine kinase DivJ to the developing cell pole. Further, we find that overexpression of the bridge protein SpmX in Caulobacter disrupts this ordered assembly, generating ectopic cell poles containing both PopZ and DivJ. Together, PopZ and SpmX assemble into a cooligomeric network that forms the basis for a polar microdomain that coordinates bacterial cell polarity.

scholarly journals E3 Ligase SCFβTrCP-induced DYRK1A Protein Degradation Is Essential for Cell Cycle Progression in HEK293 Cells

2016 ◽  
Vol 291 (51) ◽  
pp. 26399-26409 ◽  
Author(s):  
Qiang Liu ◽  
Yu Tang ◽  
Long Chen ◽  
Na Liu ◽  
Fangfang Lang ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Protein Degradation ◽  
Cell Cycle Progression ◽  
E3 Ligase ◽  
Hek293 Cells ◽  
Cycle Progression

scholarly journals Dynamic Recruitment of Nek2 Kinase to the Centrosome Involves Microtubules, PCM-1, and Localized Proteasomal Degradation

2005 ◽  
Vol 16 (4) ◽  
pp. 1711-1724 ◽  
Author(s):  
Rebecca S. Hames ◽  
Renarta E. Crookes ◽  
Kees R. Straatman ◽  
Andreas Merdes ◽  
Michelle J. Hayes ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Protein Kinase ◽  
Protein Degradation ◽  
Cell Cycle Progression ◽  
Proteasomal Degradation ◽  
Cycle Progression ◽  
Microtubule Binding ◽  
Multiple Processes ◽  
A Cell ◽  
Centrosomal Proteins

Centrosomes undergo dramatic changes in composition and activity during cell cycle progression. Yet mechanisms involved in recruiting centrosomal proteins are poorly understood. Nek2 is a cell cycle–regulated protein kinase required for regulation of centrosome structure at the G2/M transition. Here, we have addressed the processes involved in trafficking of Nek2 to the centrosome of human adult cells. We find that Nek2 exists in small, highly dynamic cytoplasmic particles that move to and from the centrosome. Many of these particles align along microtubules and a motif was identified in the Nek2 C-terminal noncatalytic domain that allows both microtubule binding and centrosome localization. FRAP experiments reveal that 70% of centrosomal Nek2 is rapidly turned over (t1/2 ∼ 3 s). Microtubules facilitate Nek2 trafficking to the centrosome but only over long distances. Cytoplasmic Nek2 particles colocalize in part with PCM-1 containing centriolar satellites and depletion of PCM-1 interferes with centrosomal recruitment of Nek2 and its substrate C-Nap1. Finally, we show that proteasomal degradation is necessary to allow rapid recruitment of new Nek2 molecules to the centrosome. Together, these data highlight multiple processes involved in regulating the abundance of Nek2 kinase at the centrosome including microtubule binding, the centriolar satellite component PCM-1, and localized protein degradation.

scholarly journals A balance of deubiquitinating enzymes controls cell cycle entry

2018 ◽  
Vol 29 (23) ◽  
pp. 2821-2834 ◽  
Author(s):  
Claudine E. Mapa ◽  
Heather E. Arsenault ◽  
Michelle M. Conti ◽  
Kristin E. Poti ◽  
Jennifer A. Benanti
Keyword(s):  
Cell Cycle ◽  
Protein Degradation ◽  
Cell Cycle Progression ◽  
Ubiquitin Ligases ◽  
Genetic Network ◽  
Wild Type ◽  
Deubiquitinating Enzymes ◽  
Cycle Progression ◽  
Cell Cycle Entry ◽  
The Stability

Protein degradation during the cell cycle is controlled by the opposing activities of ubiquitin ligases and deubiquitinating enzymes (DUBs). Although the functions of ubiquitin ligases in the cell cycle have been studied extensively, the roles of DUBs in this process are less well understood. Here, we used an overexpression screen to examine the specificities of each of the 21 DUBs in budding yeast for 37 cell cycle–regulated proteins. We find that DUBs up-regulate specific subsets of proteins, with five DUBs regulating the greatest number of targets. Overexpression of Ubp10 had the largest effect, stabilizing 15 targets and delaying cells in mitosis. Importantly, UBP10 deletion decreased the stability of the cell cycle regulator Dbf4, delayed the G1/S transition, and slowed proliferation. Remarkably, deletion of UBP10 together with deletion of four additional DUBs restored proliferation to near–wild-type levels. Among this group, deletion of the proteasome-associated DUB Ubp6 alone reversed the G1/S delay and restored the stability of Ubp10 targets in ubp10Δ cells. Similarly, deletion of UBP14, another DUB that promotes proteasomal activity, rescued the proliferation defect in ubp10Δ cells. Our results suggest that DUBs function through a complex genetic network in which their activities are coordinated to facilitate accurate cell cycle progression.

scholarly journals Human papillomavirus type 45 E7 is a transforming protein inducing retinoblastoma protein degradation and anchorage-independent cell cycle progression

Virology ◽  
2008 ◽  
Vol 379 (1) ◽  
pp. 20-29 ◽  
Author(s):  
Dieter Morandell ◽  
Ursula Rostek ◽  
Veronique Bouvard ◽  
Beatriz Campo-Fernández ◽  
Marc Fiedler ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Human Papillomavirus ◽  
Protein Degradation ◽  
Cell Cycle Progression ◽  
Retinoblastoma Protein ◽  
Cycle Progression
Sign in / Sign up

Export Citation Format

Share Document