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This study presents the crystal structure of a Fas-FADD complex, a central feature of the so-called death inducing signalling complex. The structure reveals a new mode of death domain interactions that allows four FADD and four Fas proteins in one complex.
Intrinsically photosensitive retinal ganglion cells sense and transmit light information to brain centres that control non-image-forming visual functions, such as the pupillary light reflex and circadian photoentrainment. This paper describes the biophysical properties of these melanopsin-containing cells. It is found that single-photons of light are sufficient to elicit large and prolonged responses.
This paper shows that Desulfitobacterium hafniense pyrrolysyl-tRNA synthetase–tRNAPyl is an orthogonal pair in vivo and in vitro. The structure of the co-complex reveals the distinct interactions of the protein and tRNA that distinguish this pair from those which function with the twenty standard amino acids.
The CBM complex has a key role in transducing signals from the antigen receptors in T and B cells to the transcription factor NF-κB during lymphocyte activation. Casein kinase 1α (CK1α) is shown to regulate the CBM complex in two opposing ways, first promoting and then subsequently terminating receptor-induced NF-κB activity and lymphocyte activation.
Here, subdiffraction-resolution STED fluorescence microscopy is used to detect the diffusion of single lipids or GPI-anchored proteins on the plasma membrane of a living cell. Tuning the probing spot area ∼70-fold below that of a confocal microscope reveals that unlike phosphoglycerolipids, sphingolipids and GPI-anchored proteins are trapped for ∼10 ms in cholesterol-mediated complexes within <20 nm space.
In vertebrates and other deuterostomes, the molecular pathway that leads to asymmetry utilizes the signalling molecule Nodal, a member of the TGF-β superfamily. But no orthologues of Nodal have been found in the other two great groups of bilaterians. This paper finds orthologues of nodal and one of its targets, Pitx, in two species of snail, and show that loss of nodal disrupts shell coiling.
Nuclear pore complexes (NPCs) serve as gateways between the nucleus and cytoplasm and allow only the transport of selected macromolecules across the nuclear envelope. NPCs are comprised of a scaffold that anchors proteins called FG-nucleoporins, which contain disordered regions that line the inner surface of the pore and extend into the lumen. This study reports the design of an artificial membrane that functions as a selective filter in allowing efficient passage of transport factors and transport factor carrying cargo that specifically bind to FG-nucleoporins.
This paper generates an iPS cell line from patients with spinal muscular atrophy, an autosomal recessive genetic disorder that is one of the most common inherited forms of neurological disease in children.