A novel frameshift truncation mutation in the V2 tail domain of KRT1 causes mild ichthyosis hystrix of Curth–Macklin

2020 ◽  
Vol 45 (6) ◽  
pp. 719-721
Author(s):  
Z. Yang ◽  
Z. Xu ◽  
N. Zhang ◽  
L. Ma
Keyword(s):  
Tail Domain ◽  
Truncation Mutation

Characterization of an Intermediate Filament Protein from the Platyhelminth, Dugesia japonica

2020 ◽  
Vol 27 (5) ◽  
pp. 432-446
Author(s):  
Akiko Yamamoto ◽  
Ken-ichiro Matsunaga ◽  
Toyoaki Anai ◽  
Hitoshi Kawano ◽  
Toshihisa Ueda ◽  
...  
Keyword(s):  
In Situ Hybridization ◽  
Immunohistochemical Analysis ◽  
Protein Characterization ◽  
Intermediate Filament Protein ◽  
Tail Domain ◽  
Animal Cells ◽  
Dugesia Japonica ◽  
Function Relationship

Background: Intermediate Filaments (IFs) are major constituents of the cytoskeletal systems in animal cells. Objective: To gain insights into the structure-function relationship of invertebrate cytoplasmic IF proteins, we characterized an IF protein from the platyhelminth, Dugesia japonica, termed Dif-1. Method: cDNA cloning, in situ hybridization, immunohistochemical analysis, and IF assembly experiments in vitro using recombinant Dif-1, were performed for protein characterization. Results: The structure deduced from the cDNA sequence showed that Djf-1 comprises 568 amino acids and has a tripartite domain structure (N-terminal head, central rod, and C-terminal tail) that is characteristic of IF proteins. Similar to nuclear IF lamins, Djf-1 contains an extra 42 residues in the coil 1b subdomain of the rod domain that is absent from vertebrate cytoplasmic IF proteins and a nuclear lamin-homology segment of approximately 105 residues in the tail domain; however, it contains no nuclear localization signal. In situ hybridization analysis showed that Djf-1 mRNA is specifically expressed in cells located within the marginal region encircling the worm body. Immunohistochemical analysis showed that Djf-1 protein forms cytoplasmic IFs located close to the microvilli of the cells. In vitro IF assembly experiments using recombinant proteins showed that Djf-1 alone polymerizes into IFs. Deletion of the extra 42 residues in the coil 1b subdomain resulted in the failure of IF formation. Conclusions: Together with data from other histological studies, our results suggest that Djf- 1 is expressed specifically in anchor cells within the glandular adhesive organs of the worm and that Djf-1 IFs may play a role in protecting the cells from mechanical stress.

scholarly journals Caspase Cleavage of Keratin 18 and Reorganization of Intermediate Filaments during Epithelial Cell Apoptosis

1997 ◽  
Vol 138 (6) ◽  
pp. 1379-1394 ◽  
Author(s):  
Carlos Caulín ◽  
Guy S. Salvesen ◽  
Robert G. Oshima
Keyword(s):  
Intermediate Filaments ◽  
Cleavage Site ◽  
Uv Light ◽  
Tail Domain ◽  
Proteolytic Fragment ◽  
Intermediate Filament Proteins ◽  
Caspase Cleavage ◽  
Structural Cell ◽  
Caspase 6

Keratins 8 (K8) and 18 (K18) are major components of intermediate filaments (IFs) of simple epithelial cells and tumors derived from such cells. Structural cell changes during apoptosis are mediated by proteases of the caspase family. During apoptosis, K18 IFs reorganize into granular structures enriched for K18 phosphorylated on serine 53. K18, but not K8, generates a proteolytic fragment during drug- and UV light–induced apoptosis; this fragment comigrates with K18 cleaved in vitro by caspase-6, -3, and -7. K18 is cleaved by caspase-6 into NH2-terminal, 26-kD and COOH-terminal, 22-kD fragments; caspase-3 and -7 additionally cleave the 22-kD fragment into a 19-kD fragment. The cleavage site common for the three caspases was the sequence VEVD/A, located in the conserved L1-2 linker region of K18. The additional site for caspases-3 and -7 that is not cleaved efficiently by caspase-6 is located in the COOH-terminal tail domain of K18. Expression of K18 with alanine instead of serine at position 53 demonstrated that cleavage during apoptosis does not require phosphorylation of serine 53. However, K18 with a glutamate instead of aspartate at position 238 was resistant to proteolysis during apoptosis. Furthermore, this cleavage site mutant appears to cause keratin filament reorganization in stably transfected clones. The identification of the L1-2 caspase cleavage site, and the conservation of the same or very similar sites in multiple other intermediate filament proteins, suggests that the processing of IFs during apoptosis may be initiated by a similar caspase cleavage.

scholarly journals Phosphorylation of neurofilament H subunit at the tail domain by CDC2 kinase dissociates the association to microtubules.

1991 ◽  
Vol 266 (32) ◽  
pp. 21798-21803 ◽  
Author(s):  
S. Hisanaga ◽  
M. Kusubata ◽  
E. Okumura ◽  
T. Kishimoto
Keyword(s):  
Tail Domain ◽  
Cdc2 Kinase

scholarly journals Giant conductivity of mobile non-oxide domain walls

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
S. Ghara ◽  
K. Geirhos ◽  
L. Kuerten ◽  
P. Lunkenheimer ◽  
V. Tsurkan ◽  
...  
Keyword(s):  
Magnetic Fields ◽  
Domain Wall ◽  
Domain Walls ◽  
Building Blocks ◽  
External Fields ◽  
Tail Domain ◽  
Oxide Electronics ◽  
Domain Wall Mobility ◽  
Conductance Changes ◽  
Wall Mobility

AbstractAtomically sharp domain walls in ferroelectrics are considered as an ideal platform to realize easy-to-reconfigure nanoelectronic building blocks, created, manipulated and erased by external fields. However, conductive domain walls have been exclusively observed in oxides, where domain wall mobility and conductivity is largely influenced by stoichiometry and defects. Here, we report on giant conductivity of domain walls in the non-oxide ferroelectric GaV4S8. We observe conductive domain walls forming in zig-zagging structures, that are composed of head-to-head and tail-to-tail domain wall segments alternating on the nanoscale. Remarkably, both types of segments possess high conductivity, unimaginable in oxide ferroelectrics. These effectively 2D domain walls, dominating the 3D conductance, can be mobilized by magnetic fields, triggering abrupt conductance changes as large as eight orders of magnitude. These unique properties demonstrate that non-oxide ferroelectrics can be the source of novel phenomena beyond the realm of oxide electronics.

scholarly journals The structurally disordered paramyxovirus nucleocapsid protein tail domain is a regulator of the mRNA transcription gradient

2017 ◽  
Vol 3 (2) ◽  
pp. e1602350 ◽  
Author(s):  
Robert M. Cox ◽  
Stefanie A. Krumm ◽  
Vidhi D. Thakkar ◽  
Maximilian Sohn ◽  
Richard K. Plemper
Keyword(s):  
Nucleocapsid Protein ◽  
Tail Domain ◽  
Mrna Transcription

scholarly journals Milder phenotype with SCN1A truncation mutation other than SMEI

Seizure ◽  
2010 ◽  
Vol 19 (7) ◽  
pp. 443-445 ◽  
Author(s):  
Mei-Juan Yu ◽  
Yi-Wu Shi ◽  
Mei-Mei Gao ◽  
Wei-Yi Deng ◽  
Xiao-Rong Liu ◽  
...  
Keyword(s):  
Truncation Mutation
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