Cell cycle-dependent dynamics of a plant intermediate filament motif protein with intracellular localization related to microtubules

PROTOPLASMA ◽  
2020 ◽  
Vol 257 (5) ◽  
pp. 1387-1400 ◽  
Author(s):  
Hikaru Utsunomiya ◽  
Masayuki Fujita ◽  
Fumio Naito ◽  
Tsuyoshi Kaneta
Keyword(s):  
Cell Cycle ◽  
Intermediate Filament ◽  
Intracellular Localization ◽  
Cycle Dependent

scholarly journals Pendulin, a Drosophila protein with cell cycle-dependent nuclear localization, is required for normal cell proliferation.

1995 ◽  
Vol 129 (6) ◽  
pp. 1491-1507 ◽  
Author(s):  
P Küssel ◽  
M Frasch
Keyword(s):  
Cell Cycle ◽  
Cell Proliferation ◽  
Nuclear Localization ◽  
Growth Regulation ◽  
Tandem Repeats ◽  
Sequence Similarity ◽  
Intracellular Localization ◽  
Abnormal Development ◽  
Embryonic Cells ◽  
Cycle Dependent

We describe the dynamic intracellular localization of Drosophila Pendulin and its role in the control of cell proliferation. Pendulin is a new member of a superfamily of proteins which contains Armadillo (Arm) repeats and displays extensive sequence similarities with the Srp1 protein from yeast, with RAG-1 interacting proteins from humans, and with the importin protein from Xenopus. Almost the entire polypeptide chain of Pendulin is composed of degenerate tandem repeats of approximately 42 amino acids each. A short NH2-terminal domain contains adjacent consensus sequences for nuclear localization and cdc2 kinase phosphorylation. The subcellular distribution of Pendulin is dependent on the phase of cell cycle. During interphase, Pendulin protein is exclusively found in the cytoplasm of embryonic cells. At the transition between G2 and M-phase, Pendulin rapidly translocates into the nuclei where it is distributed throughout the nucleoplasm and the areas around the chromosomes. In the larval CNS, Pendulin is predominantly expressed in the dividing neuroblasts, where it undergoes the same cell cycle-dependent redistribution as in embryos. Pendulin is encoded by the oho31 locus and is expressed both maternally and zygotically. We describe the phenotypes of recessive lethal mutations in the oho31 gene that result in a massive decrease or loss of zygotic Pendulin expression. Hematopoietic cells of mutant larvae overproliferate and form melanotic tumors, suggesting that Pendulin normally acts as a blood cell tumor suppressor. In contrast, growth and proliferation in imaginal tissues are reduced and irregular, resulting in abnormal development of imaginal discs and the CNS of the larvae. This phenotype shows that Pendulin is required for normal growth regulation. Based on the structure of the protein, we propose that Pendulin may serve as an adaptor molecule to form complexes with other proteins. The sequence similarity with importin indicates that Pendulin may play a role in the nuclear import of karyophilic proteins and some of these may be required for the normal transmission and function of proliferative signals in the cells.

scholarly journals Analysis of ERK3 intracellular localization: dynamic distribution during mitosis and apoptosis

2015 ◽  
Vol 59 (4) ◽  
Author(s):  
F. Aredia ◽  
M. Malatesta ◽  
P. Veneroni ◽  
M.G. Bottone
Keyword(s):  
Cell Cycle ◽  
Intracellular Localization ◽  
Human Tumor ◽  
Mrna Splicing ◽  
Double Immunofluorescence ◽  
Dynamic Distribution ◽  
Cell Proliferation And Differentiation ◽  
Extracellular Signal ◽  
Proliferation And Differentiation ◽  
Cycle Dependent

<p>Extracellular signal-regulated kinases (ERK) 1, 2 and 3 are involved in cell proliferation and differentiation, and apoptosis; although ERK1/2 have been widely studied, limited knowledge on ERK3 is available. The present work aimed at investigating ERK3 distribution during cell cycle and apoptosis in human tumor HeLa cells. The analysis performed by double immunofluorescence and immunoelectron microscopy experiments revealed that during interphase ERK3 is mainly resident in the nucleoplasm in association with ribonuclear proteins involved in early pre-mRNA splicing, it undergoes cell cycle-dependent redistribution and, during apoptosis, it remains in the nucleus in the form of massive nuclear aggregates, then moves to the cytoplasm and is finally extruded.</p>

scholarly journals The RNA Binding Activity of a Ribosome Biogenesis Factor, Nucleophosmin/B23, Is Modulated by Phosphorylation with a Cell Cycle-dependent Kinase and by Association with Its Subtype

2002 ◽  
Vol 13 (6) ◽  
pp. 2016-2030 ◽  
Author(s):  
Mitsuru Okuwaki ◽  
Masafumi Tsujimoto ◽  
Kyosuke Nagata
Keyword(s):  
Cell Cycle ◽  
Ribosome Biogenesis ◽  
Cellular Localization ◽  
Rna Binding ◽  
Intracellular Localization ◽  
Binding Activity ◽  
Cyclin B ◽  
Cycle Dependent

Nucleophosmin/B23 is a nucleolar phosphoprotein. It has been shown that B23 binds to nucleic acids, digests RNA, and is localized in nucleolar granular components from which preribosomal particles are transported to cytoplasm. The intracellular localization of B23 is significantly changed during the cell cycle. Here, we have examined the cellular localization of B23 proteins and the effect of mitotic phosphorylation of B23.1 on its RNA binding activity. Two splicing variants of B23 proteins, termed B23.1 and B23.2, were complexed both in vivo and in vitro. The RNA binding activity of B23.1 was impaired by hetero-oligomer formation with B23.2. Both subtypes of B23 proteins were phosphorylated during mitosis by cyclin B/cdc2. The RNA binding activity of B23.1 was repressed through cyclin B/cdc2-mediated phosphorylation at specific sites in B23. Thus, the RNA binding activity of B23.1 is stringently modulated by its phosphorylation and subtype association. Interphase B23.1 was mainly localized in nucleoli, whereas B23.2 and mitotic B23.1, those of which were incapable of binding to RNA, were dispersed throughout the nucleoplasm and cytoplasm, respectively. These results suggest that nucleolar localization of B23.1 is mediated by its ability to associate with RNA.

scholarly journals Interdependent Polar Localization of FlhF and FlhG and Their Importance for Flagellum Formation of Vibrio parahaemolyticus

2021 ◽  
Vol 12 ◽  
Author(s):  
Erick Eligio Arroyo-Pérez ◽  
Simon Ringgaard
Keyword(s):  
Cell Cycle ◽  
Vibrio Parahaemolyticus ◽  
Intracellular Localization ◽  
Dependent Manner ◽  
Swimming Ability ◽  
Polar Localization ◽  
Cell Pole ◽  
A Cell ◽  
Cycle Dependent ◽  
Spatiotemporal Localization

Failure of the cell to properly regulate the number and intracellular positioning of their flagella, has detrimental effects on the cells’ swimming ability. The flagellation pattern of numerous bacteria is regulated by the NTPases FlhF and FlhG. In general, FlhG controls the number of flagella produced, whereas FlhF coordinates the position of the flagella. In the human pathogen Vibrio parahaemolyticus, its single flagellum is positioned and formed at the old cell pole. Here, we describe the spatiotemporal localization of FlhF and FlhG in V. parahaemolyticus and their effect on swimming motility. Absence of either FlhF or FlhG caused a significant defect in swimming ability, resulting in absence of flagella in a ΔflhF mutant and an aberrant flagellated phenotype in ΔflhG. Both proteins localized to the cell pole in a cell cycle-dependent manner, but displayed different patterns of localization throughout the cell cycle. FlhF transitioned from a uni- to bi-polar localization, as observed in other polarly flagellated bacteria. Localization of FlhG was strictly dependent on the cell pole-determinant HubP, while polar localization of FlhF was HubP independent. Furthermore, localization of FlhF and FlhG was interdependent and required for each other’s proper intracellular localization and recruitment to the cell pole. In the absence of HubP or FlhF, FlhG forms non-polar foci in the cytoplasm of the cell, suggesting the possibility of a secondary localization site within the cell besides its recruitment to the cell poles.

Cell cycle dependent modulation of insulin and IGF I receptor binding to human Burkitt type ALL cells

1987 ◽  
Vol 116 (3_Suppl) ◽  
pp. S81
Author(s):  
U. VETTER ◽  
W. HARTMANN ◽  
H. HITZLER ◽  
W. HEIT ◽  
J. SCHLICKENRIEDER ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Receptor Binding ◽  
Igf I ◽  
Cycle Dependent
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