scholarly journals Molecular cloning and cell-cycle-dependent expression of a novel NIMA (never-in-mitosis in Aspergillus nidulans)-related protein kinase (TpNrk) in Tetrahymena cells

1998 ◽  
Vol 334 (1) ◽  
pp. 197-203 ◽  
Author(s):  
Shulin WANG ◽  
Shigeru NAKASHIMA ◽  
Hideki SAKAI ◽  
Osamu NUMATA ◽  
Kenta FUJIU ◽  
...  
Keyword(s):  
Heat Treatment ◽  
Cell Cycle ◽  
Cell Division ◽  
Protein Kinase ◽  
Cold Stress ◽  
Aspergillus Nidulans ◽  
Catalytic Domain ◽  
Signal Transduction Pathway ◽  
Related Protein ◽  
Synchronous Cell

With the intention of investigating the signal-transduction pathway that mediates the cold-stress response in Tetrahymena, we isolated a gene that encodes a novel protein kinase of 561 amino acids, termed Tetrahymena pyriformis NIMA (never-in-mitosis in Aspergillus nidulans)-related protein kinase (TpNrk), by differential display from Tetrahymena cells exposed to temperature shift-down. TpNrk possesses an N-terminal protein kinase domain that is highly homologous with other NIMA-related protein kinases (Neks) involved in the control of the cell cycle. The TpNrk protein is 42% identical in its catalytic domain with human Nek2, 41% identical with mouse Nek1 and 37% with A. nidulans NIMA. In addition, TpNrk and these NIMA-related kinases have long, basic C-terminal extensions and are therefore similar in overall structure. In order to further explore the function of the TpNrk gene and the association of the cold stress with the cell cycle of Tetrahymena,changes of TpNrk mRNA were determined during the course of the synchronous cell division induced by the intermittent heat treatment. The level of TpNrk transcription increased immediately after the end of the heat treatment, with a peak at 30 min, and declined thereafter reaching the minimum level when nearly 80% of the cells synchronously entered cell division (75 min after the end of heat treatment). The accumulation of TpNrk mRNA starting from 0 min to 30 min after the end of the heat treatment was assumed to be a prerequisite for the start of synchronous cell division. These results suggest that TpNrk may have a role in the cell cycle of Tetrahymena, and that mRNA expression, at least, is under tight cell-cycle control.

scholarly journals Molecular cloning and cell-cycle-dependent expression of the acetyl-CoA synthetase gene in Tetrahymena cells

1999 ◽  
Vol 343 (2) ◽  
pp. 479-485 ◽  
Author(s):  
Shulin WANG ◽  
Shigeru NAKASHIMA ◽  
Osamu NUMATA ◽  
Kenta FUJIU ◽  
Yoshinori NOZAWA
Keyword(s):  
Heat Treatment ◽  
Cell Cycle ◽  
Cell Division ◽  
Amino Acid ◽  
Mrna Expression ◽  
Mrna Level ◽  
Cyclic Heat Treatment ◽  
Acetyl Coa ◽  
Synchronous Cell ◽  
Cycle Dependent

To identify transcriptionally regulated mediators associated with the cell cycle, we adopted the differential mRNA display technique for cell cultures of Tetrahymenapyriformis synchronized by cyclic heat treatment. One cDNA fragment that was expressed differently during synchronous cell division had a greatly decreased expression at 30 min after the end of heat treatment (EHT). Using this fragment as a probe, we isolated the full-length cDNA for T. pyriformis acetyl-CoA synthetase (TpAcs) which encodes a 651 amino acid polypeptide with a predicted molecular mass of 72.8 kDa. The deduced amino acid sequence of T. pyriformis ACS shows 42% sequence identity compared with that ofLysobacter sp. acetyl-CoA synthetase (ACS), an enzyme which catalyses the formation of acetyl-CoA from acetate via an acetyl-adenylate intermediate. The deduced sequence is also 41% and 40% identical compared with those of Pseudomonas putida and Coprinus cinereus ACS, respectively. The deduced sequence of T. pyriformis ACS also shares similar characteristics of the conserved motifs I and II in the ACS family. To further investigate the actions of the gene encoding this enzyme, mRNA expression was determined during the course of synchronized cell division in T. pyriformis. Northern blot results show that the mRNA level was dramatically decreased at 30 min after EHT prior to entering synchronous cell division (which occurs 75 min after EHT), suggesting that mRNA expression of the TpAcs was associated with the cell cycle and that the down-regulated expression of TpAcs at 30 min after EHT would be required for the initiation of the oncoming synchronous cell division in T. pyriformis.

Protein kinase cascades in meiotic and mitotic cell cycle control

1990 ◽  
Vol 68 (12) ◽  
pp. 1297-1330 ◽  
Author(s):  
Steven L. Pelech ◽  
Jasbinder S. Sanghera ◽  
Maleki Daya-Makin
Keyword(s):  
Cell Cycle ◽  
Cell Division ◽  
Protein Kinase ◽  
Tyrosine Kinases ◽  
Somatic Cells ◽  
Protein Tyrosine Kinases ◽  
Sea Star ◽  
Protein Tyrosine ◽  
Threonine Kinases ◽  
Cell Division Control

Eukaryotic cell cycle progression during meiosis and mitosis is extensively regulated by reversible protein phosphorylation. Many cell surface receptors for mitogens are ligand-stimulated protein-tyrosine kinases that control the activation of a network of cytoplasmic and nuclear protein-serine(threonine) kinases. Over 30 plasma membrane associated protein-tyrosine kinases are encoded by proto-oncogenes, i.e., genes that have the potential to facilitate cancer when disregulated. Proteins such as ribosomal protein S6, microtubule-associated protein-2, myelin basic protein, and casein have been used to detect intracellular protein-serine(threonine) kinases that are activated further downstream in growth factor signalling transduction cascades. Genetic analysis of yeast cell division control (cdc) mutants has revealed another 20 or so protein-serine(threonine) kinases. One of these, specified by the cdc-2 gene in Schizosaccharomyces pombe, has homologs that are stimulated during M phase in maturing sea star and frog oocytes and mammalian somatic cells. Furthermore, during meiotic maturation in these echinoderm and amphibian oocytes, this is followed by activation of many of the same protein-serine(threonine) kinases that are stimulated when quiescent mammalian somatic cells are prompted with mitogens to traverse from G0 to G1 phase. These findings imply that a similar protein kinase cascade may oversee progression at multiple points in the cell cycle.Key words: protein kinases, mitosis, meiosis, oncogenes, cell division control.

scholarly journals Coupling of Cell Division and Differentiation in Arabidopsis thaliana Cultured Cells with Interaction of Ethylene and ABA Signaling Pathways

Life ◽  
2020 ◽  
Vol 10 (2) ◽  
pp. 15
Author(s):  
Novikova ◽  
Stepanchenko ◽  
Zorina ◽  
Nosov ◽  
Rakitin ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Signal Transduction ◽  
Arabidopsis Thaliana ◽  
Cell Division ◽  
Cell Differentiation ◽  
Signal Transduction Pathway ◽  
Transduction Pathway ◽  
Aba Signaling ◽  
Exogenous Aba ◽  
Ethylene Signal

Recent studies indicate direct links between molecular cell cycle and cell differentiation machineries. Ethylene and abscisic acid (ABA) are known to affect cell division and differentiation, but the mechanisms of such effects are poorly understood. As ethylene and ABA signaling routes may interact, we examined their involvement in cell division and differentiation in cell tissue cultures derived from several Arabidopsis thaliana plants: wild type (Col-0), and ethylene-insensitive mutants etr1-1, ctr1-1, and ein2-1. We designed an experimental setup to analyze the growth-related parameters and molecular mechanisms in proliferating cells upon short exposure to ABA. Here, we provide evidence for the ethylene–ABA signaling pathways’ interaction in the regulation of cell division and differentiation as follows: (1) when the ethylene signal transduction pathway is functionally active (Col-0), the cells actively proliferate, and exogenous ABA performs its function as an inhibitor of DNA synthesis and division; (2) if the ethylene signal is not perceived (etr1-1), then, in addition to cell differentiation (tracheary elements formation), cell death can occur. The addition of exogenous ABA can rescue the cells via increasing proliferation; (3) if the ethylene signal is perceived, but not transduced (ein2-1), then cell differentiation takes place—the latter is enhanced by exogenous ABA while cell proliferation is reduced; (4) when the signal transduction pathway is constitutively active, the cells begin to exit the cell cycle and proceed to endo-reduplication (ctr1-1). In this case, the addition of exogenous ABA promotes reactivation of cell division.

Investigating the Protein Kinase C Polarized Growth‐Related Protein Complex in Aspergillus nidulans

2020 ◽  
Vol 34 (S1) ◽  
pp. 1-1
Author(s):  
Loretta Jackson-Hayes ◽  
Alexis Craft ◽  
Muhammad Hameed ◽  
Zariah Hines ◽  
W. Toler Freyaldenhoven ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Aspergillus Nidulans ◽  
Protein Complex ◽  
Polarized Growth ◽  
Related Protein ◽  
Kinase C

scholarly journals VITAMIN B12 AND THE MACROMOLECULAR COMPOSITION OF EUGLENA

1973 ◽  
Vol 57 (3) ◽  
pp. 668-674 ◽  
Author(s):  
Pamela Leban Johnston ◽  
Edgar F. Carell
Keyword(s):  
Cell Cycle ◽  
Cell Division ◽  
Dna Synthesis ◽  
Vitamin B12 ◽  
Protein Content ◽  
Euglena Gracilis ◽  
Cell Divisions ◽  
Synchronous Cell ◽  
A Minor ◽  
Macromolecular Composition

When vitamin B12 is added to B12-deficient cultures of Euglena gracilis, the cells undergo two relatively synchronous cell divisions within a shorter than usual period of time, apparently as a result of a transitory shortening of the cell cycle. The first cell division pulse, occurring 4.5 h after addition of B12, is preceded by the completion of DNA duplication, but appears to involve no net synthesis of RNA or protein. Before the second round of cell division at about 11 h, a significant amount of DNA synthesis is observed. This time it is accompanied by a minor increase in the RNA and protein content of the culture. The cellular contents of RNA and protein were observed to decrease steadily after the resumption of cell division in B12-depleted cultures receiving the vitamin. Ultimately all three macromolecules returned to their nondeficient, plateau stage levels; by this time, cell division had ceased.

scholarly journals The ubiquitin-associated domain of AMPK-related protein kinases allows LKB1-induced phosphorylation and activation

2006 ◽  
Vol 394 (3) ◽  
Author(s):  
Mark H. Rider
Keyword(s):  
Protein Kinase ◽  
Protein Kinases ◽  
Molecular Mechanisms ◽  
Catalytic Domain ◽  
Related Protein ◽  
Biochemical Journal ◽  
Kinase Catalytic Domain ◽  
Uba Domain ◽  
Amp Activated Protein Kinase

The AMPK (AMP-activated protein kinase)-related protein kinase subfamily of the human kinome comprises 12 members closely related to the catalytic α1/α2 subunits of AMPK. The precise role of the AMPK-related kinases and their in vivo substrates is rather unclear at present, but some are involved in regulating cell polarity, whereas others appear to control cellular differentiation. Of the 12 human AMPK-related protein kinase family members, 11 can be activated following phosphorylation of their T-loop threonine residue by the LKB1 complex. Nine of these AMPK-related kinases activated by LKB1 contain an UBA (ubiquitin-associated) domain immediately C-terminal to the kinase catalytic domain. In this issue of the Biochemical Journal, Jaleel et al. show that the presence of an UBA domain in AMP-related kinases allows LKB1-induced phosphorylation and activation. The findings have implications for understanding the molecular mechanisms of activation of this fascinating family of protein kinases. Also, mutations in the UBA domains of the AMP-related kinase genes might be present in families with Peutz–Jehgers syndrome and in other cancer patients.

Interaction of the pelle kinase with the membrane-associated protein tube is required for transduction of the dorsoventral signal in Drosophila embryos

Development ◽  
1995 ◽  
Vol 121 (7) ◽  
pp. 2209-2218 ◽  
Author(s):  
R.L. Galindo ◽  
D.N. Edwards ◽  
S.K. Gillespie ◽  
S.A. Wasserman
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase ◽  
Catalytic Domain ◽  
Drosophila Embryo ◽  
Related Protein ◽  
Yeast Two Hybrid ◽  
Dorsoventral Polarity ◽  
Intracellular Signal ◽  
Two Hybrid ◽  
Drosophila Embryos

Within the Drosophila embryo, tube and the protein kinase pelle transduce an intracellular signal generated by the transmembrane receptor Toll. This signal directs import of the rel-related protein dorsal into ventral and ventrolateral nuclei, thereby establishing dorsoventral polarity. We show by immunolocalization that tube protein associates with the plasma membrane during interphase. We also find that tube sequences required for signaling interact with pelle in a yeast two-hybrid assay. We demonstrate that fusion of the pelle catalytic domain to the transmembrane receptor torso is sufficient to induce ventral fates; this activity is independent of Toll or tube. Lastly, we find that fusion of the tube protein to torso also induces ventral fates, but only in the presence of functional pelle. We propose a model wherein tube activates pelle by recruiting it to the plasma membrane, thereby propagating the axis-determining signal.

scholarly journals Inhibition of Protein Kinase B (PKB) and PKCζ Mediates Keratin K10-Induced Cell Cycle Arrest

2001 ◽  
Vol 21 (21) ◽  
pp. 7449-7459 ◽  
Author(s):  
Jesus M. Paramio ◽  
Carmen Segrelles ◽  
Sergio Ruiz ◽  
José L. Jorcano
Keyword(s):  
Cell Cycle ◽  
Signal Transduction ◽  
Protein Kinase ◽  
Cell Cycle Progression ◽  
Protein Kinase B ◽  
Signal Transduction Pathway ◽  
Cytoskeletal Proteins ◽  
Physical Interaction ◽  
Specific Expression ◽  
Phosphoinositide 3 Kinase

ABSTRACT The intermediate filament cytoskeleton is composed of keratins in all epithelial cells and imparts mechanical integrity to these cells. However, beyond this shared function, the functional significance of the carefully regulated tissue- and differentiation-specific expression of the large keratin family of cytoskeletal proteins remains unclear. We recently demonstrated that expression of keratin K10 or K16 may regulate the phosphorylation of the retinoblastoma protein (pRb), inhibiting (K10) or stimulating (K16) cell proliferation (J. M. Paramio, M. L. Casanova, C. Segrelles, S. Mittnacht, E. B. Lane, and J. L. Jorcano, Mol. Cell. Biol. 19:3086–3094, 1999). Here we show that keratin K10 function as a negative modulator of cell cycle progression involves changes in the phosphoinositide 3-kinase (PI-3K) signal transduction pathway. Physical interaction of K10 with Akt (protein kinase B [PKB]) and atypical PKCζ causes sequestration of these kinases within the cytoskeleton and inhibits their intracellular translocation. As a consequence, the expression of K10 impairs the activation of PKB and PKCζ. We also demonstrate that this inhibition impedes pRb phosphorylation and reduces the expression of cyclins D1 and E. Functional and biochemical data also demonstrate that the interaction between K10 and these kinases involves the non-α-helical amino domain of K10 (NTerm). Together, these results suggest new and essential roles for the keratins as modulators of specific signal transduction pathways.

Sign in / Sign up

Export Citation Format

Share Document