<oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:creator>Hartenstein, Volker</dc:creator>
  <dc:creator>Yuan, Michaela</dc:creator>
  <dc:creator>Younossi-Hartenstein, Amelia</dc:creator>
  <dc:creator>Karandikar, Aanavi</dc:creator>
  <dc:creator>Bernardo-Garcia, F. Javier</dc:creator>
  <dc:creator>Sprecher, Simon G.</dc:creator>
  <dc:creator>Knust, Elisabeth</dc:creator>
  <dc:date>2019-09-01</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">Photoreceptor cells (PRCs) across the animal kingdom are characterized by a  stacking of apical membranes to accommodate the high abundance of photopigment.  In arthropods and many other invertebrate phyla PRC membrane stacks adopt the  shape of densely packed microvilli that form a structure called rhabdomere. PRCs and  surrounding accessory cells, including pigment cells and lens-forming cells, are  grouped in stereotyped units, the ommatidia. In larvae of holometabolan insects, eyes  (called stemmata) are reduced in terms of number and composition of ommatidia. The  stemma of Drosophila (Bolwig organ) is reduced to a bilateral cluster of subepidermal  PRCs, lacking all other cell types. In the present paper we have analyzed the  development and fine structure of the Drosophila larval PRCs. Shortly after their  appearance in the embryonic head ectoderm, PRC precursors delaminate and lose  expression of apical markers of epithelial cells, including Crumbs and several  centrosome-associated proteins. In the early first instar larva, PRCs show an  expanded, irregularly shaped apical surface that is folded into multiple horizontal  microvillar-like processes (MLPs). Apical PRC membranes and MLPs are covered  with a layer of extracellular matrix. MLPs are predominantly aligned along an axis that  extends ventro-anteriorly to dorso-posteriorly, but vary in length, diameter, and  spacing. Individual MLPs present a “beaded” shape, with thick segments (0.2–0.3 μm  diameter) alternating with thin segments (&gt;0.1 μm). We show that loss of the  glycoprotein Chaoptin, which is absolutely essential for rhabdomere formation in the  adult PRCs, does not lead to severe abnormalities in larval PRCs.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://folia.unifr.ch/global/documents/308106</dc:identifier>
  <dc:identifier>https://folia.unifr.ch/documents/308106/files/spr_sem.pdf</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1016/j.ydbio.2019.05.017</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:rights>License undefined</dc:rights>
  <dc:source>Developmental Biology. - 2019, vol. 453, no. 1, p. 56–67</dc:source>
  <dc:subject>info:eu-repo/classification/udc/57</dc:subject>
  <dc:title xmlns:ns1="xml" ns1:lang="en">Serial electron microscopic reconstruction of the drosophila larval eye: Photoreceptors with a rudimentary rhabdomere of microvillar-like processes</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>
