Protein domains and disease-causing mutations in the myotubularin, amphiphysin, and dynamin families.

<p>Myotubularin contains a PH-GRAM domain that may bind lipids and a coil-coiled-PDZ binding site to form homo- and hetero-dimers with other members of the myotubularin family. Only the disease-causing missense mutations in MTM1 are represented, based on the international UMD-MTM1 database, existing currently in a local version in Strasbourg (France). MTM1 mutations identified in more than two patients are R69C(9 families), P205L(5), V227M(3), R241C(13), G378R(4), E404K(4), and Y397C(5). AMPH1 and BIN1 possess an N-BAR domain able to sense and eventually curve membrane and a C-terminal SH3 domain binding to proteins with proline-rich domains, such as dynamins <a href="http://www.plosgenetics.org/article/info:doi/10.1371/journal.pgen.1002595#pgen.1002595-Peter1" target="_blank">[48]</a>, <a href="http://www.plosgenetics.org/article/info:doi/10.1371/journal.pgen.1002595#pgen.1002595-Owen1" target="_blank">[88]</a>. In addition some isoforms have clathrin-binding and Myc-binding domains (CBD, MBD); a phosphoinositide-binding motif is present between the BAR and MBD domains specifically in skeletal muscle. DNM2 contains a GTPase domain, a central middle (MID) domain, a Pleckstrin Homology (PH) domain, a GTPase Effector Domain (GED), and a C-terminal Proline Rich Domain (PRD). Dominant mutations in DNM2 lead to either centronuclear myopathy (above), or peripheral CMT neuropathy (below). Only coding mutations are listed for all genes.</p

Cellular functions of myotubularins, amphiphysins, and dynamins implicated in human diseases and their related pathological mechanisms.

<p>(A) Human diseases, (B) their related pathological mechanisms. Membrane fission is necessary for vesicle formation and subsequent trafficking, while inhibition of membrane fission or membrane addition at the T-tubules in muscle may be necessary for their formation and maintenance.</p

Phylogenetic relationships.

<p>Phylogenetic relationships within the amphiphysin (A), dynamin (B), and myotubularin (C) protein families. Sequences were collected using the eggNOG database, which groups genes into families at different taxonomic levels. A high quality multiple sequence alignment was computed for each protein family on all proteins members including, respectively, 91 myotubularin protein sequences, 23 dynamin protein sequences, and 13 amphiphysin protein sequences. For a more detailed description, see <a href="http://www.plosgenetics.org/article/info:doi/10.1371/journal.pgen.1002595#pgen.1002595.s001" target="_blank">Protocol S1</a>. Scale represents the percentage of divergence.</p

Myotubularin/amphiphysin/dynamin protein functions in specific tissues, based on animal and cell models.

<p>Myotubularin/amphiphysin/dynamin protein functions in specific tissues, based on animal and cell models.</p

Design and evaluation of Actichip, a thematic microarray for the study of the actin cytoskeleton-0

<p><b>Copyright information:</b></p><p>Taken from "Design and evaluation of Actichip, a thematic microarray for the study of the actin cytoskeleton"</p><p>http://www.biomedcentral.com/1471-2164/8/294</p><p>BMC Genomics 2007;8():294-294.</p><p>Published online 29 Aug 2007</p><p>PMCID:PMC2077341.</p><p></p>3 replicates per RNA sample), the human oligonucleotide Operon set (4 replicates) and the Actichip arrays (10 replicates). Experiments were carried out using the same lots of RNAs extracted from human carcinoma MCF-7 cell line and from human skeletal muscle. Data were analysed as stated in the "Methods" section resulting in two groups of genes : "detected" and "not detected". The genes found similarly expressed or not expressed in less than 2/3 of the replicated assays were deemed "non reproducible". The histograms show the distribution of the three groups of genes for each platform relative to the samples. Results are expressed as percentages relative to the total number of genes simultaneously represented on each array platform

Spray-Deposited Anisotropic Assemblies of Plasmonic Nanowires for Direction-Sensitive Strain Measurement

The development of nanoscale composites with hierarchical architecture and complex anisotropies enables the fabrication of new classes of devices. Stretchable strain sensors have been developed in the past for applications in various fields such as wearable electronics and soft robotics, yet the sensing capacities of most of these sensors are independent of the direction of deformation. In the present work, we report on the preparation of a direction-sensitive strain sensor using the anisotropic optical properties of a monolayer of oriented plasmonic 1D nano-objects. Grazing incidence spraying (GIS) is used for depositing a monolayer of in-plane aligned silver nanowires with a controlled density on a deformable and transparent substrate. Using the selective excitation of transverse and longitudinal localized plasmon resonance modes of silver nanowires by polarized UV–visible–NIR spectroscopy, we show that the macroscopic anisotropic properties of the monolayer upon stretching are highly dependent on the stretching direction and light polarization. Measuring the polarized optical properties of the anisotropic thin films upon stretching thus allow for retrieving both the local strain and the direction of the deformation using a simple model

Additional file 5: of Uncommon nucleotide excision repair phenotypes revealed by targeted high-throughput sequencing

Clinical pictures of patients #8 (A) and #9 (B) (mutated in ERCC8(CSA)). (PPTX 403 kb