Pkd1l1 establishes left-right asymmetry and physically interacts with Pkd2

Development. 2011 Mar;138(6):1131-42. doi: 10.1242/dev.058149. Epub 2011 Feb 9.

Abstract

In mammals, left-right (L-R) asymmetry is established by posteriorly oriented cilia driving a leftwards laminar flow in the embryonic node, thereby activating asymmetric gene expression. The two-cilia hypothesis argues that immotile cilia detect and respond to this flow through a Pkd2-mediated mechanism; a putative sensory partner protein has, however, remained unidentified. We have identified the Pkd1-related locus Pkd1l1 as a crucial component of L-R patterning in mouse. Systematic comparison of Pkd1l1 and Pkd2 point mutants reveals strong phenocopying, evidenced by both morphological and molecular markers of sidedness; both mutants fail to activate asymmetric gene expression at the node or in the lateral plate and exhibit right isomerism of the lungs. Node and cilia morphology were normal in mutants and cilia demonstrated typical motility, consistent with Pkd1l1 and Pkd2 activity downstream of nodal flow. Cell biological analysis reveals that Pkd1l1 and Pkd2 localise to the cilium and biochemical experiments demonstrate that they can physically interact. Together with co-expression in the node, these data argue that Pkd1l1 is the elusive Pkd2 binding partner required for L-R patterning and support the two-cilia hypothesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Body Patterning / genetics*
  • Body Patterning / physiology
  • Cells, Cultured
  • Cilia / genetics
  • Cilia / metabolism
  • Cilia / physiology
  • Gene Expression Regulation, Developmental
  • Humans
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism
  • Membrane Proteins / physiology*
  • Mice
  • Mice, Inbred C3H
  • Mice, Inbred C57BL
  • Mice, Transgenic
  • Models, Biological
  • Models, Molecular
  • Molecular Sequence Data
  • Polymorphism, Single Nucleotide / genetics
  • Polymorphism, Single Nucleotide / physiology
  • Protein Binding / genetics
  • Protein Binding / physiology
  • Sequence Homology, Amino Acid
  • TRPP Cation Channels / genetics
  • TRPP Cation Channels / metabolism*
  • TRPP Cation Channels / physiology

Substances

  • Membrane Proteins
  • Pkd1l1 protein, mouse
  • TRPP Cation Channels
  • polycystic kidney disease 2 protein