Diversity in insect axis formation: two
            orthodenticle
            genes and
            hunchback
            act in anterior patterning and influence dorsoventral organization in the honeybee (
            Apis mellifera
            )

Megan J. Wilson; Peter K. Dearden

doi:10.1242/dev.067926

Diversity in insect axis formation: two orthodenticle genes and hunchback act in anterior patterning and influence dorsoventral organization in the honeybee ( Apis mellifera )

Development ◽

10.1242/dev.067926 ◽

2011 ◽

Vol 138 (16) ◽

pp. 3497-3507 ◽

Cited By ~ 29

Author(s):

Megan J. Wilson ◽

Peter K. Dearden

Keyword(s):

Apis Mellifera ◽

Axis Formation ◽

Anterior Patterning

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Differentiation Processes of the Ocellar Retina of the Honeybee (Apis Mellifera L.)

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100159692 ◽

1990 ◽

Vol 48 (3) ◽

pp. 430-431

Author(s):

Maria Anna Pabst

Keyword(s):

Apis Mellifera ◽

Distal Part ◽

Cell Layer ◽

Single Layer ◽

Photoreceptor Cells ◽

Distal Segment ◽

Compound Eyes ◽

Thin Sections ◽

Ultrastructural Studies ◽

Adult Worker

In addition to the compound eyes, honeybees have three dorsal ocelli on the vertex of the head. Each ocellus has about 800 elongated photoreceptor cells. They are paired and the distal segment of each pair bears densely packed microvilli forming together a platelike fused rhabdom. Beneath a common cuticular lens a single layer of corneagenous cells is present.Ultrastructural studies were made of the retina of praepupae, different pupal stages and adult worker bees by thin sections and freeze-etch preparations. In praepupae the ocellar anlage consists of a conical group of epidermal cells that differentiate to photoreceptor cells, glial cells and corneagenous cells. Some photoreceptor cells are already paired and show disarrayed microvilli with circularly ordered filaments inside. In ocelli of 2-day-old pupae, when a retinogenous and a lentinogenous cell layer can be clearly distinguished, cell membranes of the distal part of two photoreceptor cells begin to interdigitate with each other and so start to form the definitive microvilli. At the beginning the microvilli often occupy the whole width of the developing rhabdom (Fig. 1).

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Centrosome Aurora A gradient ensures single polarity axis in C. elegans embryos

Biochemical Society Transactions ◽

10.1042/bst20200298 ◽

2020 ◽

Vol 48 (3) ◽

pp. 1243-1253 ◽

Cited By ~ 1

Author(s):

Sukriti Kapoor ◽

Sachin Kotak

Keyword(s):

Symmetry Breaking ◽

Cell Fate ◽

Cell Cortex ◽

Axis Formation ◽

Aurora A Kinase ◽

Aurora A ◽

C Elegans ◽

Cell Embryo ◽

Polarity Establishment

Cellular asymmetries are vital for generating cell fate diversity during development and in stem cells. In the newly fertilized Caenorhabditis elegans embryo, centrosomes are responsible for polarity establishment, i.e. anterior–posterior body axis formation. The signal for polarity originates from the centrosomes and is transmitted to the cell cortex, where it disassembles the actomyosin network. This event leads to symmetry breaking and the establishment of distinct domains of evolutionarily conserved PAR proteins. However, the identity of an essential component that localizes to the centrosomes and promotes symmetry breaking was unknown. Recent work has uncovered that the loss of Aurora A kinase (AIR-1 in C. elegans and hereafter referred to as Aurora A) in the one-cell embryo disrupts stereotypical actomyosin-based cortical flows that occur at the time of polarity establishment. This misregulation of actomyosin flow dynamics results in the occurrence of two polarity axes. Notably, the role of Aurora A in ensuring a single polarity axis is independent of its well-established function in centrosome maturation. The mechanism by which Aurora A directs symmetry breaking is likely through direct regulation of Rho-dependent contractility. In this mini-review, we will discuss the unconventional role of Aurora A kinase in polarity establishment in C. elegans embryos and propose a refined model of centrosome-dependent symmetry breaking.

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