Reptilian skin is covered with scales forming armor that makes it watertight and enables reptiles to live on land in contrast to amphibians. An important part of the skin is the horny epidermis, with thick stratum corneum in which waxes are arranged in membrane-like layers. In lizards and snakes, the whole skin is covered in overlapping epidermal scales and in turtles and crocodiles in dermal scutes. The cornified part of the epidermis is strengthened by β-keratin and sometimes α-keratin. In crocodiles and many turtles, the outer scale surface consists of β-keratin and the hinge region containing α-keratin. In lizards and snakes, both keratins form continuous layers with the α-keratin below the β-keratin. Some reptiles have developed a sensitive mechanosensory system in the skin. The colors of reptile skin are produced by melanocytes and three types of chromatophores: melanophores, xanthophores, and iridophores. The color patterns may be fixed or the chromatophores may provide rapid color change. Skin from different species of reptiles, turtles (red-eared slider (Trachemys scripta elegans)), snakes (Emerald tree boa (Corallus caninus) and Burmese python (Python bivittatus)), Cuvier’s dwarf caiman (Paleosuchus palpebrosus), lizards (Leopard Gecko (Eublepharis macularius)), and Green iguana (Iguana iguana), were examined with histology techniques and compared.

The type 2 dopamine receptor D₂ (D₂-R), member of the G protein-coupled receptor (GPCR) superfamily, exists in two isoforms, short (D_2S-R) and long (D_2L-R). They differ by an additional 29 amino acids (AA) in the third cytoplasmic loop (ICL3) of the D_2L-R. These isoforms differ in their intracellular localization and trafficking functionality, as D_2L-R possesses a larger intracellular pool, mostly in the endoplasmic reticulum (ER). This review focuses on the evolutionarily conserved motifs in the ICL3 of the D₂-R and proteins interacting with the ICL3 of both isoforms, specifically with the 29 AA insert. These motifs might be involved in D₂-R exit from the ER and have an impact on cell-surface and intracellular localization and, therefore, also play a role in the function of dopamine receptor signaling, ligand binding and possible homo/heterodimerization. Our recent bioinformatic data on potential new interaction partners for the ICL3 of D₂-Rs are also presented. Both are highly relevant, and have clinical impacts on the pathophysiology of several diseases such as Parkinson’s disease, schizophrenia, Tourette’s syndrome, Huntington’s disease, manic depression, and others, as they are connected to a variety of essential motifs and differences in communication with interaction partners.

This study examined whether the conserved arginine cluster present within the 29-amino acid insert of the long form of the D₂ dopamine receptor (D_2L-R) confers its predominant intracellular localization. We hypothesized that the conserved arginine cluster (RRR) located within the insert could act as an RXR-type endoplasmic reticulum (ER) retention signal. Arginine residues (R) within the cluster at positions 267, 268, and 269 were charge-reserved to glutamic acids (E), either individually or in clusters, thus generating single, double, and triple D_2L-R mutants. Through analyses of cellular localization by confocal microscopy and enzyme-linked immunosorbent assay (ELISA), radioligand binding assay, bioluminescence resonance energy transfer (BRET²) β-arrestin 2 (βarr2) recruitment assay, and cAMP signaling, it was revealed that charge reversal of the R residues at all three positions within the motif impaired their colocalization with ER marker calnexin and led to significantly improved cell surface expression. Additionally, these data demonstrate that an R to glutamic acid (E) substitution at position 2 within the RXR motif is not functionally permissible. Furthermore, all generated D_2L-R mutants preserved their functional integrity regarding ligand binding, agonist-induced βarr2 recruitment and Gα_i-mediated signaling. In summary, our results show that the conserved arginine cluster within the 29-amino acid insert of third cytoplasmic loop (IC3) of the D_2L-R appears to be the ER retention signal.

Background: The viral G-protein-coupled receptor (vGPCR) BILF1 encoded by the Epstein–Barr virus (EBV) is an oncogene and immunoevasin and can downregulate MHC-I molecules at the surface of infected cells. MHC-I downregulation, which presumably occurs through co-internalization with EBV-BILF1, is preserved among BILF1 receptors, including the three BILF1 orthologs encoded by porcine lymphotropic herpesviruses (PLHV BILFs). This study aimed to understand the detailed mechanisms of BILF1 receptor constitutive internalization, to explore the translational potential of PLHV BILFs compared with EBV-BILF1.Methods: A novel real-time fluorescence resonance energy transfer (FRET)-based internalization assay combined with dominant-negative variants of dynamin-1 (Dyn K44A) and the chemical clathrin inhibitor Pitstop2 in HEK-293A cells was used to study the effect of specific endocytic proteins on BILF1 internalization. Bioluminescence resonance energy transfer (BRET)-saturation analysis was used to study BILF1 receptor interaction with β-arrestin2 and Rab7. In addition, a bioinformatics approach informational spectrum method (ISM) was used to investigate the interaction affinity of BILF1 receptors with β-arrestin2, AP-2, and caveolin-1.Results: We identified dynamin-dependent, clathrin-mediated constitutive endocytosis for all BILF1 receptors. The observed interaction affinity between BILF1 receptors and caveolin-1 and the decreased internalization in the presence of a dominant-negative variant of caveolin-1 (Cav S80E) indicated the involvement of caveolin-1 in BILF1 trafficking. Furthermore, after BILF1 internalization from the plasma membrane, both the recycling and degradation pathways are proposed for BILF1 receptors.Conclusions: The similarity in the internalization mechanisms observed for EBV-BILF1 and PLHV1-2 BILF1 provide a foundation for further studies exploring a possible translational potential for PLHVs, as proposed previously, and provides new information about receptor trafficking.Graphical

Introduction: The morphological characteristics of eyes in fishes are highly diverse and have evolved to meet the specific visual requirements as per their habitats. These morphological features of eyes are important for researchers and ecologists. The dusky spinefoot (Siganus luridus) is a tropical teleost fish with a laterally flattened body which lives in the Mediterranean Sea. Currently, there are no histological data relating to the Siganus luridus eye.Methods: In this study, the morphology of the Siganus luridus eye was examined to enhance our understanding of its structure and its relationship to fish ecology. Detailed gross and microscopic features were recorded using light and scanning microscopy.Results: The key observations describe the main structural features of the eye of Siganus luridus, specifically, the diameter of the orbit, architecture of three tunics of eye and detailed lens description. The choroid was divided into four layers, and had a rete mirabile, consisting of numerous small blood vessels in the choroidal gland. The tapetum lucidum was observed, which is interesting since Siganus luridus is herbivore and herbivores typically lack a tapetum lucidum.Discussion: These observations shed new light on the intricate eye structure of Siganus luridus and provide valuable insights into its visual abilities and adaptations to the aquatic environment and feeding behavior.

Satisfactory investigations of the equine foot appear to be limited by the histo-morphological complexity of internal hoof structures. Foot lameness is considered to be one of the most debilitating pathological disorders of the equine foot. In most species, foot lameness is traditionally linked to hoof deformity, and a set of molecular events have been defined in relation to the disease. So far, there is controversy regarding the incidence of foot lameness in horses, as it is unclear whether it is foot lameness that triggers hoof distortions or vice-versa. In order to develop a better understanding of foot lameness, we review both the healthy and lame foot anatomy, cell biology and vascularisation and using micro-computed tomography show new methods of visualising internal structures within the equine foot.