Novel nonsense mutation inMSX1in familial nonsyndromic oligodontia: subcellular localization and role of homeodomain/MH4

2013 ◽  
Vol 122 (1) ◽  
pp. 15-20 ◽  
Author(s):  
Masashi Kimura ◽  
Junichiro Machida ◽  
Seishi Yamaguchi ◽  
Akio Shibata ◽  
Tadashi Tatematsu ◽  
...  
Keyword(s):  
Subcellular Localization ◽  
Nonsense Mutation

The role of the glyoxylate cycle in the symbiotic fungus Tuber borchii: expression analysis and subcellular localization

2007 ◽  
Vol 52 (3-4) ◽  
pp. 159-170 ◽  
Author(s):  
Simona Abba’ ◽  
Raffaella Balestrini ◽  
Alessandra Benedetto ◽  
Hanspeter Rottensteiner ◽  
José Ramón De Lucas ◽  
...  
Keyword(s):  
Subcellular Localization ◽  
Expression Analysis ◽  
Glyoxylate Cycle ◽  
Tuber Borchii ◽  
Symbiotic Fungus ◽  
The Glyoxylate Cycle

Ypsilon Schachtel, aDrosophilaY-box protein, acts antagonistically to Orb in theoskarmRNA localization and translation pathway

Development ◽  
2002 ◽  
Vol 129 (1) ◽  
pp. 197-209 ◽  
Author(s):  
Jennifer H. Mansfield ◽  
James E. Wilhelm ◽  
Tulle Hazelrigg
Keyword(s):  
Subcellular Localization ◽  
Essential Role ◽  
Genetic Interaction ◽  
Mrna Localization ◽  
Rna Localization ◽  
Essential Step ◽  
Positive Regulator ◽  
Body Patterning ◽  
Translational Regulators

Subcellular localization of mRNAs within the Drosophila oocyte is an essential step in body patterning. Yps, a Drosophila Y-box protein, is a component of an ovarian ribonucleoprotein complex that also contains Exu, a protein that plays an essential role in mRNA localization. Y-box proteins are known translational regulators, suggesting that this complex might regulate translation as well as mRNA localization. Here we examine the role of the yps gene in these events. We show that yps interacts genetically with orb, a positive regulator of oskar mRNA localization and translation. The nature of the genetic interaction indicates that yps acts antagonistically to orb. We demonstrate that Orb protein is physically associated with both the Yps and Exu proteins, and that this interaction is mediated by RNA. We propose a model wherein Yps and Orb bind competitively to oskar mRNA with opposite effects on translation and RNA localization.

scholarly journals The inlA Gene of Listeria monocytogenesLO28 Harbors a Nonsense Mutation Resulting in Release of Internalin

1998 ◽  
Vol 66 (7) ◽  
pp. 3420-3422 ◽  
Author(s):  
Renaud Jonquières ◽  
Hélène Bierne ◽  
Jérôme Mengaud ◽  
Pascale Cossart
Keyword(s):  
Cell Adhesion ◽  
Listeria Monocytogenes ◽  
Virulence Factor ◽  
Adhesion Molecule ◽  
Nonsense Mutation ◽  
Cell Adhesion Molecule ◽  
Culture Medium ◽  
Surface Protein ◽  
Truncated Protein

ABSTRACT Internalin is a surface protein that mediates entry ofListeria monocytogenes EGD into epithelial cells expressing the cell adhesion molecule human E-cadherin or its chicken homolog, L-CAM, which act as receptors for internalin. After observing that entry of L. monocytogenes LO28 into S180 fibroblasts, in contrast to that of EGD, did not increase after transfection with L-CAM, we examined both the expression and the structure of internalin in strain LO28. We discovered a nonsense mutation in inlA which results in a truncated protein released in the culture medium. Mutations leading to release of internalin were also detected in clinical and food isolates. These results question the role of internalin as a virulence factor in murine listeriosis.

Evidence for a role of the N-terminal domain in subcellular localization of the neuronal connexin36 (Cx36)

2002 ◽  
Vol 69 (4) ◽  
pp. 448-465 ◽  
Author(s):  
G. Zoidl ◽  
C. Meier ◽  
E. Petrasch-Parwez ◽  
C. Zoidl ◽  
H.-W. Habbes ◽  
...  
Keyword(s):  
Subcellular Localization ◽  
Terminal Domain

Inhibition of p300 suppresses growth of breast cancer. Role of p300 subcellular localization

2014 ◽  
Vol 97 (3) ◽  
pp. 411-424 ◽  
Author(s):  
María E. Fermento ◽  
Norberto A. Gandini ◽  
Débora G. Salomón ◽  
María J. Ferronato ◽  
Cristian A. Vitale ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Subcellular Localization

scholarly journals α-Secretase nonsense mutation (ADAM10 Tyr167*) in familial Alzheimer’s disease

2020 ◽  
Vol 12 (1) ◽  
Author(s):  
Pablo Agüero ◽  
María José Sainz ◽  
María-Salud García-Ayllón ◽  
Javier Sáez-Valero ◽  
Raquel Téllez ◽  
...  
Keyword(s):  
Nonsense Mutation ◽  
Genetic Model ◽  
Late Onset ◽  
Future Research ◽  
Clinical Genetic ◽  
Csf Analysis ◽  
Amyloidogenic Processing ◽  
Age Related ◽  
Spanish Cohort

Abstract Background The disintegrin metalloproteinase 10 (ADAM10) is the main α-secretase acting in the non-amyloidogenic processing of APP. Some ADAM10 gene variants have been associated with higher susceptibility to develop late-onset AD, though clear clinical-genetic correlates remain elusive. Methods Clinical-genetic and biomarker study of a first family with early- and late-onset AD associated with a nonsense ADAM10 mutation (p.Tyr167*). CSF analysis included AD core biomarkers, as well as Western blot of ADAM10 species and sAPPα and sAPPβ peptides. We evaluate variant’s pathogenicity, pattern of segregation, and further screened for the p.Tyr167* mutation in 197 familial AD cases from the same cohort, 200 controls from the same background, and 274 AD cases from an independent Spanish cohort. Results The mutation was absent from public databases and segregated with the disease. CSF Aβ42, total tau, and phosphorylated tau of affected siblings were consistent with AD. The predicted haploinsufficiency effect of the nonsense mutation was supported by (a) ADAM10 isoforms in CSF decreased around 50% and (b) 70% reduction of CSF sAPPα peptide, both compared to controls, while sAPPβ levels remained unchanged. Interestingly, sporadic AD cases had a similar decrease in CSF ADAM10 levels to that of mutants, though their sAPPα and sAPPβ levels resembled those of controls. Therefore, a decreased sAPPα/sAPPβ ratio was an exclusive feature of mutant ADAM10 siblings. The p.Tyr167* mutation was not found in any of the other AD cases or controls screened. Conclusions This family illustrates the role of ADAM10 in the amyloidogenic process and the clinical development of the disease. Similarities between clinical and biomarker findings suggest that this family could represent a genetic model for sporadic late-onset AD due to age-related downregulation of α-secretase. This report encourages future research on ADAM10 enhancers.

Dynamics of the subcellular localization of RalBP1/RLIP through the cell cycle: the role of targeting signals and of protein‐protein interactions

2012 ◽  
Vol 26 (5) ◽  
pp. 2164-2174 ◽  
Author(s):  
Jonathan Fillatre ◽  
Delphine Delacour ◽  
Lucie Van Hove ◽  
Thomas Bagarre ◽  
Nathalie Houssin ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Subcellular Localization ◽  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Targeting Signals
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