The Role of a Cell Surface Inhibitor in Early Signal Transduction Associated with the Regulation of Cell Division and Differentiation

1992 ◽  
Vol 95 (1/2) ◽  
pp. 11 ◽  
Author(s):  
Terry C. Johnson ◽  
Daniel J. Enebo ◽  
Philip J. Moos ◽  
Heideh K. Fattaey
Keyword(s):  
Signal Transduction ◽  
Cell Division ◽  
Cell Surface ◽  
Early Signal ◽  
A Cell

Inhibition of DNA synthesis and cell division by a cell surface sialoglycopeptide

1989 ◽  
Vol 139 (2) ◽  
pp. 269-274 ◽  
Author(s):  
Heideh Fattaey ◽  
Terry C. Johnson ◽  
Hsin-Hwei Chou
Keyword(s):  
Cell Division ◽  
Cell Surface ◽  
Dna Synthesis ◽  
A Cell ◽  
Inhibition Of Dna Synthesis

ROLE OF CELL SURFACE COMPONENTS AND RECEPTORS IN THROMBIN-STIMULATED CELL DIVISION

1982 ◽  
pp. 43-59
Author(s):  
Dennis D. Cunningham ◽  
Darrel H. Carney ◽  
Joffre B. Baker ◽  
David A. Low ◽  
Kevin C. Glenn
Keyword(s):  
Cell Division ◽  
Cell Surface

scholarly journals SET8 prevents excessive DNA methylation by methylation-mediated degradation of UHRF1 and DNMT1

2019 ◽  
Author(s):  
Huifang Zhang ◽  
Qinqin Gao ◽  
Shuo Tan ◽  
Jia You ◽  
Cong Lyu ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Dna Methylation ◽  
Cell Division ◽  
Global Dna Methylation ◽  
Protein Methylation ◽  
Accessory Factor ◽  
Protein Methyltransferase ◽  
A Cell ◽  
Do So

Abstract Faithful inheritance of DNA methylation across cell division requires DNMT1 and its accessory factor UHRF1. However, how this axis is regulated to ensure DNA methylation homeostasis remains poorly understood. Here we show that SET8, a cell-cycle-regulated protein methyltransferase, controls protein stability of both UHRF1 and DNMT1 through methylation-mediated, ubiquitin-dependent degradation and consequently prevents excessive DNA methylation. SET8 methylates UHRF1 at lysine 385 and this modification leads to ubiquitination and degradation of UHRF1. In contrast, LSD1 stabilizes both UHRF1 and DNMT1 by demethylation. Importantly, SET8 and LSD1 oppositely regulate global DNA methylation and do so most likely through regulating the level of UHRF1 than DNMT1. Finally, we show that UHRF1 downregulation in G2/M by SET8 has a role in suppressing DNMT1-mediated methylation on post-replicated DNA. Altogether, our study reveals a novel role of SET8 in promoting DNA methylation homeostasis and identifies UHRF1 as the hub for tuning DNA methylation through dynamic protein methylation.

scholarly journals Neisseria gonorrhoeae Porin P1.B Induces Endosome Exocytosis and a Redistribution of Lamp1 to the Plasma Membrane

2002 ◽  
Vol 70 (11) ◽  
pp. 5965-5971 ◽  
Author(s):  
Patricia Ayala ◽  
Brandi Vasquez ◽  
Lee Wetzler ◽  
Magdalene So
Keyword(s):  
Plasma Membrane ◽  
Epithelial Cells ◽  
Cell Surface ◽  
Neisseria Gonorrhoeae ◽  
Bacterial Infection ◽  
Immunoglobulin A ◽  
Late Endosomes ◽  
A Cell ◽  
Iga Protease

ABSTRACT The immunoglobulin A (IgA) protease secreted by pathogenic Neisseria spp. cleaves Lamp1, thereby altering lysosomes in a cell and promoting bacterial intracellular survival. We sought to determine how the IgA protease gains access to cellular Lamp1 in order to better understand the role of this cleavage event in bacterial infection. In a previous report, we demonstrated that the pilus-induced Ca2+ transient triggers lysosome exocytosis in human epithelial cells. This, in turn, increases the level of Lamp1 at the plasma membrane, where it can be cleaved by IgA protease. Here, we show that porin also induces a Ca2+ flux in epithelial cells. This transient is similar in nature to that observed in phagocytes exposed to porin. In contrast to the pilus-induced Ca2+ transient, the porin-induced event does not trigger lysosome exocytosis. Instead, it stimulates exocytosis of early and late endosomes and increases Lamp1 on the cell surface. These results indicate that Neisseria pili and porin perturb Lamp1 trafficking in epithelial cells by triggering separate and distinct Ca2+-dependent exocytic events, bringing Lamp1 to the cell surface, where it can be cleaved by IgA protease.

scholarly journals Genetic Characterization of a Cell Envelope-Associated Proteinase from Lactobacillus helveticus CNRZ32

1999 ◽  
Vol 181 (15) ◽  
pp. 4592-4597 ◽  
Author(s):  
Jeffrey A. Pederson ◽  
Gerald J. Mileski ◽  
Bart C. Weimer ◽  
James L. Steele
Keyword(s):  
Cell Surface ◽  
Deletion Mutant ◽  
Cell Envelope ◽  
Physiological Role ◽  
Lactobacillus Helveticus ◽  
Whole Cells ◽  
A Cell ◽  
Hydrolysis Of

ABSTRACT A cell envelope-associated proteinase gene (prtH) was identified in Lactobacillus helveticus CNRZ32. TheprtH gene encodes a protein of 1,849 amino acids and with a predicted molecular mass of 204 kDa. The deduced amino acid sequence of the prtH product has significant identity (45%) to that of the lactococcal PrtP proteinases. Southern blot analysis indicates thatprtH is not broadly distributed within L. helveticus. A prtH deletion mutant of CNRZ32 was constructed to evaluate the physiological role of PrtH. PrtH is not required for rapid growth or fast acid production in milk by CNRZ32. Cell surface proteinase activity and specificity were determined by hydrolysis of αs1-casein fragment 1-23 by whole cells. A comparison of CNRZ32 and its prtH deletion mutant indicates that CNRZ32 has at least two cell surface proteinases that differ in substrate specificity.

Phyllotaxis Turns over a New Leaf – A Review

2019 ◽  
Author(s):  
Derek T Lamport ◽  
Li Tan ◽  
Michael Held ◽  
Marcia Kieliszewski
Keyword(s):  
Cell Surface ◽  
Calcium Binding ◽  
Wall Stress ◽  
Protein Chemistry ◽  
Computer Prediction ◽  
Cell Wall Stress ◽  
A Cell ◽  
Ancient Problem ◽  
General Explanation

Sixty years ago in the lab adjacent to Fred Sanger (1958 Nobel Prize for protein chemistry), I discovered the cell surface hydroxyproline-rich glycoproteins. Nature keeps some of her secrets longer than others. It has taken many years to dissect the molecular function and biological role of extensins and arabinogalactan proteins (AGPs). Extensins template the formation of new cell walls. AGPs remained baffling and enigmatic until a Eureka moment when computer prediction of AGP calcium binding depicted paired glucuronic acid residues and thus the likely role of a cell surface AGP-Ca2+capacitor: In conjunction with the auxin-activated proton pump that releases bound Ca2+ it led us to formulate the Hechtian Growth Oscillator as A Global Paradigm with a pivotal role in Ca2+ homeostasis. The ramifications are profound. They cannot be shrugged off with sceptical disdain but demand critical reappraisal of current dogma. Phyllotaxis is an ancient problem; it involves an essential role for auxin and the auxin efflux “PIN” proteins together with mechanotransduction of stress-strain as phyllotactic determinants. However, a general explanation remains elusive despite much effort, particularly by mathematicians. Here we propose a novel biochemical algorithm: Hechtian oscillator transduction of cell wall stress generates phyllotactic patterns quite independent of a mathematical approach. Plants simply use different rules and follow a different route.

scholarly journals Cooperation Between the Septins and the Actomyosin Ring and Role of a Cell-Integrity Pathway During Cell Division in Fission Yeast

Genetics ◽  
2010 ◽  
Vol 186 (3) ◽  
pp. 897-915 ◽  
Author(s):  
Jian-Qiu Wu ◽  
Yanfang Ye ◽  
Ning Wang ◽  
Thomas D. Pollard ◽  
John R. Pringle
Keyword(s):  
Cell Division ◽  
Fission Yeast ◽  
Cell Integrity ◽  
A Cell

The role of yan in mediating the choice between cell division and differentiation

Development ◽  
1995 ◽  
Vol 121 (12) ◽  
pp. 3947-3958 ◽  
Author(s):  
R. Rogge ◽  
P.J. Green ◽  
J. Urano ◽  
S. Horn-Saban ◽  
M. Mlodzik ◽  
...  
Keyword(s):  
Cell Division ◽  
Growth Factor Receptor ◽  
Developmental Context ◽  
Eye Disc ◽  
A Cell ◽  
Epidermal Growth ◽  
Notch Pathways ◽  
Relationship Of ◽  
The Relationship

An allele of the yan locus was isolated as an enhancer of the Ellipse mutation of the Drosophila epidermal growth factor receptor (Egfr) gene. This yan allele is an embryonic lethal and also fails to complement the lethality of anterior open (aop) mutations. Phenotypic and complementation analysis revealed that aop is allelic to yan and genetically the lethal alleles act as null mutations for the yan gene. Analysis of the lethal alleles in the embryo and in mitotic clones showed that loss of yan function causes cells to overproliferate in the dorsal neuroectoderm of the embryo and in the developing eye disc. Our studies suggest that the role of yan is defined by the developmental context of the cells in which it functions. An important role of this gene is in allowing a cell to choose between cell division and differentiation. The relationship of the Egfr and Notch pathways to this developmental role of yan is discussed.

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