Changes in gene expression and cell shape characterise stages of epibranchial placode-derived neuron maturation in the chick.

Sensory neurons in the head are largely generated from neurogenic placodes. Previous studies have revealed early events in placode development; however, the process of maturation has not been studied. In this study, it has been shown that placodal neurogenesis follows a sequential progression with distinct stages defined by expression of specific markers. These markers highlight domains of maturation within the stream of migratory neuroblasts that extend between the placode and the neural tube. Commitment to neurogenesis occurs in the apical placode, with the newborn neuroblasts delaminating basally and entering a transition zone. The neuroblasts migrate through the transition zone, differentiating further and becoming post-mitotic as they approach the ganglionic anlage. It has further been demonstrated that this progression from the transition zone to the ganglionic anlage is accompanied by a switch from multipolar to bipolar cell morphology. This sequential progression parallels events observed elsewhere in the nervous system, but here the stages are distinct and anatomically segregated. It is proposed that placodal neurogenesis provides a tractable system to examine the transition between states in neurogenesis.

Cranial neural crest cells form corridors prefiguring sensory neuroblast migration.

The majority of cranial sensory neurons originate in placodes in the surface ectoderm, migrating to form ganglia that connect to the central nervous system (CNS). Interactions between inward-migrating sensory neuroblasts and emigrant cranial neural crest cells (NCCs) play a role in coordinating this process, but how the relationship between these two cell populations is established is not clear. Here, we demonstrate that NCCs generate corridors delineating the path of migratory neuroblasts between the placode and CNS in both chick and mouse. In vitro analysis shows that NCCs are not essential for neuroblast migration, yet act as a superior substrate to mesoderm, suggesting provision of a corridor through a less-permissive mesodermal territory. Early organisation of NCC corridors occurs prior to sensory neurogenesis and can be recapitulated in vitro; however, NCC extension to the placode requires placodal neurogenesis, demonstrating reciprocal interactions. Together, our data indicate that NCC corridors impose physical organisation for precise ganglion formation and connection to the CNS, providing a local environment to enclose migrating neuroblasts and axonal processes as they migrate through a non-neural territory.

Drosophila liquid facets-Related encodes Golgi epsin and is an essential gene required for cell proliferation, growth, and patterning.

Epsin and epsin-Related (epsinR) are multi-modular proteins that stimulate clathrin-coated vesicle formation. Epsin promotes endocytosis at the plasma membrane, and epsinR functions at the Golgi and early endosomes for trans-Golgi network/endosome vesicle trafficking. In Drosophila, endocytic epsin is known as Liquid facets, and it is essential specifically for Notch signaling. Here, by generating and analyzing loss-of-function mutants in the liquid facets-Related (lqfR) gene of Drosophila, we investigated the function of Golgi epsin in a multicellular context. We found that LqfR is indeed a Golgi protein, and that like liquid facets, lqfR is essential for Drosophila viability. In addition, primarily by analyzing mutant eye discs, we found that lqfR is required for cell proliferation, insulin-independent cell growth, and cell patterning, consistent with a role in one or several signaling pathways. Epsins in all organisms share an ENTH (epsin N-terminal homology) domain, which binds phosphoinositides enriched at the plasma membrane or the Golgi membrane. The epsinR ENTH domain is also the recognition element for particular cargos. By generating wild-type and mutant lqfR transgenes, we found that all apparent LqfR functions are independent of its ENTH domain. These results suggest that LqfR transports specific cargo critical to one or more signaling pathways, and lays the foundation for identifying those proteins.