First light for avian embryos: eggshell thickness and pigmentation mediate variation in development and UV exposure in wild bird eggs

Article first published online: 29 JUL 20141. The avian embryo's development is influenced by both the amount and the wavelength of the light that passes through the eggshell. Commercial poultry breeders use light of specific wavelengths to accelerate embryonic growth, yet the effects of the variably patterned eggshells of wild bird species on light transmission and embryonic development remain largely unexplored. 2. Here, we provide the first comparative phylogenetic analysis of light transmission, through a diverse range of bird eggshells (74 British breeding species), in relation to the eggshell's thickness, permeability, pigment concentration and surface reflectance spectrum (colour). 3. The percentage of light transmitted through the eggshell was measured in the spectral range 250–700 nm. Our quantitative analyses confirm anecdotal reports that eggshells filter the light of the externally coloured shell. Specifically, we detected a positive relationship between surface eggshell reflectance (‘brightness’) and the percentage of light transmitted through the eggshell, and this relationship was strongest at wavelengths in the human-visible blue-green region of the spectra (c. 435 nm). 4. We show that less light passes through thicker eggshells with greater total pigment concentrations. By contrast, permeability (measured as water vapour conductance) did not covary significantly with light transmission. Eggs of closed-nesting species let more light pass through, compared with open nesters. 5. We postulate that greater light transmission is required to assist embryonic development under low light exposure. Importantly, this result provides an ecological explanation for the repeated evolution of immaculate, white- or pale-coloured eggshells in species nesting in enclosed spaces. 6. Finally, we detected correlative support for the solar radiation hypothesis, in that eggshells of bird species with a longer incubation period let significantly less of the potentially harmful, ultraviolet (UV) light pass through the eggshell. In summary, we demonstrate suites of avian eggshell properties, including eggshell structure and pigmentation, which are consistent with an evolutionary pressure to both enhance and protect embryonic development.Golo Maurer, Steven J. Portugal, Mark E. Hauber, Ivan Mikšík, Douglas G. D. Russell and Phillip Casse

Heavy and light roles: myosin in the morphogenesis of the heart

Myosin is an essential component of cardiac muscle, from the onset of cardiogenesis through to the adult heart. Although traditionally known for its role in energy transduction and force development, recent studies suggest that both myosin heavy-chain and myosin lightchain proteins are required for a correctly formed heart. Myosins are structural proteins that are not only expressed from early stages of heart development, but when mutated in humans they may give rise to congenital heart defects. This review will discuss the roles of myosin, specifically with regards to the developing heart. The expression of each myosin protein will be described, and the effects that altering expression has on the heart in embryogenesis in different animal models will be discussed. The human molecular genetics of the myosins will also be reviewed

Structural basis for ALK2/BMPR2 receptor complex signaling through kinase domain oligomerization

Upon ligand binding, bone morphogenetic protein (BMP) receptors form active tetrameric complexes, comprised of two type I and two type II receptors, which then transmit signals to SMAD proteins. The link between receptor tetramerization and the mechanism of kinase activation, however, has not been elucidated. Here, using hydrogen deuterium exchange mass spectrometry (HDX-MS), small angle X-ray scattering (SAXS) and molecular dynamics (MD) simulations, combined with analysis of SMAD signaling, we show that the kinase domain of the type I receptor ALK2 and type II receptor BMPR2 form a heterodimeric complex via their C-terminal lobes. Formation of this dimer is essential for ligand-induced receptor signaling and is targeted by mutations in BMPR2 in patients with pulmonary arterial hypertension (PAH). We further show that the type I/type II kinase domain heterodimer serves as the scaffold for assembly of the active tetrameric receptor complexes to enable phosphorylation of the GS domain and activation of SMADs.This article is published as Agnew, C., Ayaz, P., Kashima, R. et al. Structural basis for ALK2/BMPR2 receptor complex signaling through kinase domain oligomerization. Nat Commun 12, 4950 (2021). https://doi.org/10.1038/s41467-021-25248-5. © The Author(s) 2021. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/ licenses/by/4.0/

Competition for binding between veratridine and KIFMK: an open channel blocking peptide of the RIIA sodium channel

Veratridine, an alkaloid isolated from the rhizome of V. album, binds and slows the inactivation of the brain sodium channels. The synthetic pentapeptide KIFMK causes a voltage- and use-dependent open-channel block of the RIIA (rat brain type IIA) sodium channel (Eaholtz, Scheuer & Catterall, 1994). Our studies on the RIIA sodium channel expressed in CHO cells reveal that the fraction of veratridine modified sodium channels decreases linearly with increasing KIFMK concentration. However, the time constant for dissociation of veratridine from the channel remains unchanged in the presence of a high concentration of KIFMK, as opposed to that in the presence of QX314 where the dissociation appears to be more complex. These data are consistent with mutually exclusive binding of the open channel blocking peptide and veratridine to the brain sodium channel

Voltage dependent gating of veratridine modified RIIA Na<SUP>+</SUP>channel α-subunit expressed heterologously in CHO cells

The voltage-dependent kinetics of veratridine-modified RIIA Na<SUP>+</SUP> channel a subunit expressed heterologously in CHO cells were studied using the whole-cell patch-clamp technique. The activation and deactivation kinetics are well described by double exponential functions but poorly by a monoexponential function. Unlike the slow component, the fast time constant and associated amplitude factor depended steeply on the potential. The steady-state activation of veratridine-modified channels is described by a Boltzmann function with a V <SUB>½</SUB> of -131.9 mV and a slope of 9.41 mV. A two-state model is proposed for the fast component that explains the kinetics of veratridine's mechanism of action

Tetrapentylammonium block of chloramine-T and veratridine modified rat brain type iia sodium channels

Tetrapentylammonium (TPeA) block of rat brain type IIA sodium channel alpha subunit was studied using whole cell patch clamp. Results indicate that TPeA blocks the inactivating brain sodium channel in a potential and use-dependent manner similar to that of the cardiac sodium channel. Removal of inactivation using chloramine-T (CT) unmasks a time-dependent block by TPeA consistent with slow blocking kinetics. On the other hand, no time dependence is observed when inactivation is abolished by modification with veratridine. TPeA does not bind in a potential-dependent fashion to veratridine-modified channels and does not significantly affect gating of veratridine-modified channels suggesting that high affinity binding of TPeA to the brain sodium channel is lost after veratridine modificatio