scholarly journals RHO Effector Domain

2020 ◽  
Author(s):  
Keyword(s):  
Effector Domain

scholarly journals Muropeptide Binding and the X-ray Structure of the Effector Domain of the Transcriptional Regulator AmpR ofPseudomonas aeruginosa

2017 ◽  
Vol 139 (4) ◽  
pp. 1448-1451 ◽  
Author(s):  
David A. Dik ◽  
Teresa Domínguez-Gil ◽  
Mijoon Lee ◽  
Dusan Hesek ◽  
Byungjin Byun ◽  
...  
Keyword(s):  
Transcriptional Regulator ◽  
Effector Domain ◽  
X Ray

scholarly journals The Effector Domain of Myristoylated Alanine-rich C Kinase Substrate Binds Strongly to Phosphatidylinositol 4,5-Bisphosphate

2000 ◽  
Vol 276 (7) ◽  
pp. 5012-5019 ◽  
Author(s):  
Jiyao Wang ◽  
Anna Arbuzova ◽  
Gyöngyi Hangyás-Mihályné ◽  
Stuart McLaughlin
Keyword(s):  
Effector Domain ◽  
Kinase Substrate

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 Identification of a novel effector domain of BIN1 for cancer suppression

2011 ◽  
Vol 112 (10) ◽  
pp. 2992-3001 ◽  
Author(s):  
Greta L. Lundgaard ◽  
Natae E. Daniels ◽  
Slovénie Pyndiah ◽  
Erica K. Cassimere ◽  
Kazi M. Ahmed ◽  
...  
Keyword(s):  
Effector Domain ◽  
Cancer Suppression

scholarly journals Sequestration of phosphoinositides by mutated MARCKS effector domain inhibits stimulated Ca2+mobilization and degranulation in mast cells

2011 ◽  
Vol 22 (24) ◽  
pp. 4908-4917 ◽  
Author(s):  
Deepti Gadi ◽  
Alice Wagenknecht-Wiesner ◽  
David Holowka ◽  
Barbara Baird
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Time Course ◽  
Fluorescent Protein ◽  
Immunoglobulin E ◽  
Dependent Manner ◽  
Effector Domain ◽  
Granule Exocytosis ◽  
Kinase C

Protein kinase C β (PKCβ) participates in antigen-stimulated mast cell degranulation mediated by the high-affinity receptor for immunoglobulin E, FcεRI, but the molecular basis is unclear. We investigated the hypothesis that the polybasic effector domain (ED) of the abundant intracellular substrate for protein kinase C known as myristoylated alanine-rich protein kinase C substrate (MARCKS) sequesters phosphoinositides at the inner leaflet of the plasma membrane until MARCKS dissociates after phosphorylation by activated PKC. Real-time fluorescence imaging confirms synchronization between stimulated oscillations of intracellular Ca2+concentrations and oscillatory association of PKCβ–enhanced green fluorescent protein with the plasma membrane. Similarly, MARCKS-ED tagged with monomeric red fluorescent protein undergoes antigen-stimulated oscillatory dissociation and rebinding to the plasma membrane with a time course that is synchronized with reversible plasma membrane association of PKCβ. We find that MARCKS-ED dissociation is prevented by mutation of four serine residues that are potential sites of phosphorylation by PKC. Cells expressing this mutated MARCKS-ED SA4 show delayed onset of antigen-stimulated Ca2+mobilization and substantial inhibition of granule exocytosis. Stimulation of degranulation by thapsigargin, which bypasses inositol 1,4,5-trisphosphate production, is also substantially reduced in the presence of MARCKS-ED SA4, but store-operated Ca2+entry is not inhibited. These results show the capacity of MARCKS-ED to regulate granule exocytosis in a PKC-dependent manner, consistent with regulated sequestration of phosphoinositides that mediate granule fusion at the plasma membrane.

scholarly journals Variable Virulence of Biotype 3Vibrio vulnificusdue to MARTX Toxin Effector Domain Composition

mSphere ◽  
2017 ◽  
Vol 2 (4) ◽  
Author(s):  
Byoung Sik Kim ◽  
Hannah E. Gavin ◽  
Karla J. F. Satchell
Keyword(s):  
Food Chain ◽  
Vibrio Vulnificus ◽  
Infectious Agent ◽  
High Morbidity ◽  
Effector Domain ◽  
Content Type ◽  
Human Food ◽  
Effector Domains ◽  
Human Food Chain ◽  
Natural Hosts

ABSTRACTVibrio vulnificusis an environmental organism that causes septic human infections characterized by high morbidity and mortality. The annual incidence and global distribution of this pathogen are increasing as ocean waters warm. Clinical strains exhibit variations in the primary virulence toxin, suggesting a potential for the emergence of new strains with altered virulence properties. A clonal outbreak of tilapia-associated wound infections in Israel serves as a natural experiment for the sudden emergence of a newV. vulnificusstrain. The effector domain content of the multifunctional autoprocessing RTX (MARTX) toxin of the outbreak-associated biotype 3 (BT3) strains was previously shown to harbor a modification generated by recombination. The modification introduced an actin-induced adenylate cyclase effector domain (ExoY) and an effector domain that disrupts the Golgi organelle (DmX). Here, we report that the exchange of these effector domains for a putative progenitor biotype 1 toxin arrangement produces a toxin that slows the lysis kinetics of targeted epithelial cells but increases cellular rounding phenotypes in response to bacteria. In addition, replacing the biotype 3 toxin variant with the putative progenitor biotype 1 variant renders the resulting strain significantly more virulent in mice. This suggests that the exchange of MARTX effector domains during the emergence of BT3 generated a toxin with reduced toxin potency, resulting in decreased virulence of this outbreak-associated strain. We posit that selection for reduced virulence may serve as a route for this lethal infectious agent to enter the human food chain by allowing it to persist in natural hosts.IMPORTANCEVibrio vulnificusis a serious infection linked to climate change. The virulence capacity of these bacteria can vary by gene exchange, resulting in new variants of the primary virulence toxin. In this study, we tested whether the emergence of an epidemic strain ofV. vulnificuswith a novel toxin variant correlated with a change in virulence. We found that restoring the biotype 3 toxin variant to the putative progenitor-type toxin resulted in dramatically increased virulence, revealing that the emergence of the biotype 3 strain could be linked to virulence reduction. This reduced virulence, previously found also in the biotype 1 strain, suggests that reduced virulence may stimulate outbreaks, as strains have greater capacity to enter the human food chain through reduced impact to environmental hosts.

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