Ablepharon and craniosynostosis in a patient with a localized TWIST1 basic domain substitution

2018 ◽  
Vol 176 (12) ◽  
pp. 2777-2780
Author(s):  
Toshiki Takenouchi ◽  
Yoshiaki Sakamoto ◽  
Hironori Sato ◽  
Hisato Suzuki ◽  
Tomoko Uehara ◽  
...  
Keyword(s):  
Basic Domain

scholarly journals Transduction of Cu,Zn-superoxide dismutase mediated by an HIV-1 Tat protein basic domain into mammalian cells

FEBS Letters ◽  
2000 ◽  
Vol 485 (2-3) ◽  
pp. 163-167 ◽  
Author(s):  
Hyeok Yil Kwon ◽  
Won Sik Eum ◽  
Hyun Woo Jang ◽  
Jung Hoon Kang ◽  
Jiyoon Ryu ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Mammalian Cells ◽  
Tat Protein ◽  
Basic Domain ◽  
Hiv 1

scholarly journals Identification and isotropy characterization of deformed random fields through excursion sets

2018 ◽  
Vol 50 (3) ◽  
pp. 706-725
Author(s):  
Julie Fournier
Keyword(s):  
Random Field ◽  
Euler Characteristic ◽  
Random Fields ◽  
Weak Form ◽  
Invariance Property ◽  
Basic Domain ◽  
Excursion Sets ◽  
The Mean ◽  
Isotropic Random

Abstract A deterministic application θ:ℝ2→ℝ2 deforms bijectively and regularly the plane and allows the construction of a deformed random field X∘θ:ℝ2→ℝ from a regular, stationary, and isotropic random field X:ℝ2→ℝ. The deformed field X∘θ is, in general, not isotropic (and not even stationary), however, we provide an explicit characterization of the deformations θ that preserve the isotropy. Further assuming that X is Gaussian, we introduce a weak form of isotropy of the field X∘θ, defined by an invariance property of the mean Euler characteristic of some of its excursion sets. We prove that deformed fields satisfying this property are strictly isotropic. In addition, we are able to identify θ, assuming that the mean Euler characteristic of excursion sets of X∘θ over some basic domain is known.

scholarly journals Role of the Gag Matrix Domain in Targeting Human Immunodeficiency Virus Type 1 Assembly

2000 ◽  
Vol 74 (6) ◽  
pp. 2855-2866 ◽  
Author(s):  
Akira Ono ◽  
Jan M. Orenstein ◽  
Eric O. Freed
Keyword(s):  
Human Immunodeficiency Virus ◽  
Plasma Membrane ◽  
Virus Particle ◽  
Particle Formation ◽  
Membrane Targeting ◽  
Basic Domain ◽  
Golgi Vesicles ◽  
Immunodeficiency Virus ◽  
Hiv 1

ABSTRACT Human immunodeficiency virus type 1 (HIV-1) particle formation and the subsequent initiation of protease-mediated maturation occur predominantly on the plasma membrane. However, the mechanism by which HIV-1 assembly is targeted specifically to the plasma membrane versus intracellular membranes is largely unknown. Previously, we observed that mutations between residues 84 and 88 of the matrix (MA) domain of HIV-1 Gag cause a retargeting of virus particle formation to an intracellular site. In this study, we demonstrate that the mutant virus assembly occurs in the Golgi or in post-Golgi vesicles. These particles undergo core condensation in a protease-dependent manner, indicating that virus maturation can occur not only on the plasma membrane but also in the Golgi or post-Golgi vesicles. The intracellular assembly of mutant particles is dependent on Gag myristylation but is not influenced by p6Gag or envelope glycoprotein expression. Previous characterization of viral revertants suggested a functional relationship between the highly basic domain of MA (amino acids 17 to 31) and residues 84 to 88. We now demonstrate that mutations in the highly basic domain also retarget virus particle formation to the Golgi or post-Golgi vesicles. Although the basic domain has been implicated in Gag membrane binding, no correlation was observed between the impact of mutations on membrane binding and Gag targeting, indicating that these two functions of MA are genetically separable. Plasma membrane targeting of Gag proteins with mutations in either the basic domain or between residues 84 and 88 was rescued by coexpression with wild-type Gag; however, the two groups of MA mutants could not rescue each other. We propose that the highly basic domain of MA contains a major determinant of HIV-1 Gag plasma membrane targeting and that mutations between residues 84 and 88 disrupt plasma membrane targeting through an effect on the basic domain.

scholarly journals Tat basic domain: A “Swiss army knife” of HIV-1 Tat?

2019 ◽  
Vol 29 (2) ◽  
pp. e2031 ◽  
Author(s):  
Margarita A. Kurnaeva ◽  
Eugene V. Sheval ◽  
Yana R. Musinova ◽  
Yegor S. Vassetzky
Keyword(s):  
Basic Domain ◽  
Hiv 1

scholarly journals Arginine Methylation Regulates Telomere Length and Stability

2009 ◽  
Vol 29 (18) ◽  
pp. 4918-4934 ◽  
Author(s):  
Taylor R. H. Mitchell ◽  
Kimberly Glenfield ◽  
Kajaparan Jeyanthan ◽  
Xu-Dong Zhu
Keyword(s):  
Cell Proliferation ◽  
Cancer Cells ◽  
Telomere Length ◽  
Control Cell ◽  
Arginine Methylation ◽  
Human Cells ◽  
Focus Formation ◽  
Basic Domain ◽  
Normal Human ◽  
Normal Human Cells

ABSTRACT TRF2, a component of the shelterin complex, functions to protect telomeres. TRF2 contains an N-terminal basic domain rich in glycines and arginines, similar to the GAR motif that is methylated by protein arginine methyltransferases. However, whether arginine methylation regulates TRF2 function has not been determined. Here we report that amino acid substitutions of arginines with lysines in the basic domain of TRF2 induce telomere dysfunction-induced focus formation, leading to induction of cellular senescence. We have demonstrated that cells overexpressing TRF2 lysine mutants accumulate telomere doublets, indicative of telomere instability. We uncovered that TRF2 interacts with PRMT1, and its arginines in the basic domain undergo PRMT1-mediated methylation both in vitro and in vivo. We have shown that loss of PRMT1 induces growth arrest in normal human cells but has no effect on cell proliferation in cancer cells, suggesting that PRMT1 may control cell proliferation in a cell type-specific manner. We found that depletion of PRMT1 in normal human cells results in accumulation of telomere doublets, indistinguishable from overexpression of TRF2 lysine mutants. PRMT1 knockdown in cancer cells upregulates TRF2 association with telomeres, promoting telomere shortening. Taken together, these results suggest that PRMT1 may control telomere length and stability in part through TRF2 methylation.

Evidence for a Plasma Membrane-Mediated Permeability Barrier to Tat Basic Domain in Well-Differentiated Epithelial Cells: Lack of Correlation with Heparan Sulfate†

Biochemistry ◽  
2002 ◽  
Vol 41 (42) ◽  
pp. 12652-12661 ◽  
Author(s):  
Stefania Violini ◽  
Vijay Sharma ◽  
Julie L. Prior ◽  
Mary Dyszlewski ◽  
David Piwnica-Worms
Keyword(s):  
Plasma Membrane ◽  
Epithelial Cells ◽  
Heparan Sulfate ◽  
Permeability Barrier ◽  
Basic Domain ◽  
Well Differentiated
Sign in / Sign up

Export Citation Format

Share Document