Sites of regulatory interaction between calcium ATPases and phospholamban

1997 ◽  
Vol 92 (S1) ◽  
pp. 11-15 ◽  
Author(s):  
D. H. MacLennan ◽  
T. Toyofuku ◽  
Y. Kimura
Keyword(s):  
Regulatory Interaction ◽  
Calcium Atpases

Sites of Regulatory Interaction between Calcium ATPases and Phospholambana

1998 ◽  
Vol 853 (1 CARDIAC SARCO) ◽  
pp. 31-42 ◽  
Author(s):  
DAVID H. MacLENNAN ◽  
YOSHIHIRO KIMURA ◽  
TOSHIHIKO TOYOFUKU
Keyword(s):  
Regulatory Interaction ◽  
Calcium Atpases

Introduction: Governing Regulatory Interaction: the Normative Question

2006 ◽  
Vol 12 (4) ◽  
pp. 431-439 ◽  
Author(s):  
Viktor Mayer-Schonberger ◽  
Alexander Somek
Keyword(s):  
Regulatory Interaction ◽  
Normative Question ◽  
The Normative Question

Complementation and regulatory interaction between two cloned fimbrial gene clusters of Escherichia coli strain KS71

1985 ◽  
Vol 200 (1) ◽  
pp. 60-64 ◽  
Author(s):  
Mikael Rhen ◽  
Vuokko Väisänen-Rhen ◽  
Auli Pere ◽  
Timo K. Korhonen
Keyword(s):  
Escherichia Coli ◽  
Gene Clusters ◽  
Coli Strain ◽  
Regulatory Interaction

scholarly journals Mechanism of N-Wasp Activation by Cdc42 and Phosphatidylinositol 4,5-Bisphosphate

2000 ◽  
Vol 150 (6) ◽  
pp. 1299-1310 ◽  
Author(s):  
Rajat Rohatgi ◽  
Hsin-yi Henry Ho ◽  
Marc W. Kirschner
Keyword(s):  
Binding Site ◽  
Physical Interaction ◽  
Regulatory Interaction ◽  
Actin Nucleation ◽  
Sequence Element ◽  
Effector Domain ◽  
Nucleation Activity ◽  
Syndrome Protein ◽  
Upstream Regulators ◽  
Terminal Effector

Neuronal Wiskott-Aldrich Syndrome protein (N-WASP) transmits signals from Cdc42 to the nucleation of actin filaments by Arp2/3 complex. Although full-length N-WASP is a weak activator of Arp2/3 complex, its activity can be enhanced by upstream regulators such as Cdc42 and PI(4,5)P2. We dissected this activation reaction and found that the previously described physical interaction between the NH2-terminal domain and the COOH-terminal effector domain of N-WASP is a regulatory interaction because it can inhibit the actin nucleation activity of the effector domain by occluding the Arp2/3 binding site. This interaction between the NH2- and COOH termini must be intramolecular because in solution N-WASP is a monomer. Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) influences the activity of N-WASP through a conserved basic sequence element located near the Cdc42 binding site rather than through the WASp homology domain 1. Like Cdc42, PI(4,5)P2 reduces the affinity between the NH2- and COOH termini of the molecule. The use of a mutant N-WASP molecule lacking this basic stretch allowed us to delineate a signaling pathway in Xenopus extracts leading from PI(4,5)P2 to actin nucleation through Cdc42, N-WASP, and Arp2/3 complex. In this pathway, PI(4,5)P2 serves two functions: first, as an activator of N-WASP; and second, as an indirect activator of Cdc42.

scholarly journals Structural basis for the regulatory interaction of the methylglyoxal synthase MgsA with the carbon flux regulator Crh inBacillus subtilis

2018 ◽  
Vol 293 (16) ◽  
pp. 5781-5792 ◽  
Author(s):  
Achim Dickmanns ◽  
Christopher P. Zschiedrich ◽  
Johannes Arens ◽  
Iwan Parfentev ◽  
Jan Gundlach ◽  
...  
Keyword(s):  
Carbon Flux ◽  
Structural Basis ◽  
Regulatory Interaction ◽  
Methylglyoxal Synthase

Calcium ATPases

2013 ◽  
pp. 432-439
Author(s):  
Chikashi Toyoshima
Keyword(s):  
Calcium Atpases

scholarly journals Coilin enhances phosphorylation and stability of DGCR8 and promotes miRNA biogenesis

2021 ◽  
pp. mbc.E21-05-0225
Author(s):  
Katheryn E. Lett ◽  
Madelyn K. Logan ◽  
Douglas M. McLaurin ◽  
Michael D. Hebert
Keyword(s):  
Noncoding Rnas ◽  
Mature Mirnas ◽  
Cajal Body ◽  
Mirna Biogenesis ◽  
Regulatory Interaction ◽  
Small Noncoding Rnas ◽  
Control Gene Expression ◽  
Processing Steps ◽  
Posttranscriptional Level

MicroRNAs (miRNAs) are ∼22 nt small noncoding RNAs that control gene expression at the posttranscriptional level through translational inhibition and destabilization of their target mRNAs. The biogenesis of miRNAs involves a series of processing steps beginning with cropping of the primary miRNA transcript by the Microprocessor complex, which is comprised of Drosha and DGCR8. Here we report a novel regulatory interaction between the Microprocessor components and coilin, the Cajal Body (CB) marker protein. Coilin knockdown causes alterations in the level of primary and mature miRNAs, let-7a and miR-34a, and their miRNA targets, HMGA2 and Notch1, respectively. We also found that coilin knockdown affects the levels of DGCR8 and Drosha in cells with (HeLa) and without (WI-38) CBs. To further explore the role of coilin in miRNA biogenesis, we conducted a series of co-immunoprecipitation experiments using coilin and DGCR8 constructs, which revealed that coilin and DGCR8 can form a complex. Additionally, our results indicate that phosphorylation of DGCR8, which has been shown to increase protein stability, is impacted by coilin knockdown. Collectively, our results implicate coilin as a member of the regulatory network governing miRNA biogenesis.

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