Phr1 regulates retinogeniculate targeting independent of activity and ephrin-A signalling

Mol Cell Neurosci. 2009 Jul;41(3):304-12. doi: 10.1016/j.mcn.2009.04.001. Epub 2009 Apr 14.

Abstract

Proper functioning of the mammalian visual system requires that connections between the eyes and their central targets develop precisely. At birth, axons from the two eyes project to broad, overlapping regions of the dorsal-lateral geniculate nucleus (dLGN). In the adult, retinal axons segregate into distinct monocular regions at stereotyped locations within the dLGN. This process is driven by both molecular cues and activity-dependent synaptic competition. Here we demonstrate that Phr1, an evolutionarily conserved regulator of synapse formation and axon guidance, defines a novel molecular pathway required for proper localization of retinogeniculate projections. Following conditional excision of Phr1 in the retina, eye-specific domains within the dLGN are severely disturbed, despite normal spontaneous retinal wave activity and monocular segregation. Although layer placement is dramatically altered, Phr1 mutant retinal axons respond to ephrin-A in vitro. These findings indicate that Phr1 is a key presynaptic regulator of retinogeniculate layer placement independent of activity, segregation, or ephrin-A signaling.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Axons / metabolism
  • Axons / pathology
  • Ephrins / metabolism*
  • Geniculate Bodies / abnormalities
  • Geniculate Bodies / metabolism*
  • Intracellular Signaling Peptides and Proteins / deficiency*
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Mice
  • Mice, Knockout
  • Optic Chiasm / embryology
  • Optic Chiasm / metabolism
  • Retina / embryology
  • Retina / pathology
  • Retina / physiology*
  • Signal Transduction
  • Visual Pathways / abnormalities
  • Visual Pathways / metabolism

Substances

  • Ephrins
  • Intracellular Signaling Peptides and Proteins
  • Membrane Proteins
  • Plekhb1 protein, mouse