Dynein and EFF-1 control dendrite morphology by regulating the localization pattern of SAX-7 in epidermal cells

J Cell Sci. 2017 Dec 1;130(23):4063-4071. doi: 10.1242/jcs.201699. Epub 2017 Oct 26.

Abstract

Our previous work showed that the cell adhesion molecule SAX-7 forms an elaborate pattern in Caenorhabditis elegans epidermal cells, which instructs PVD dendrite branching. However, the molecular mechanism forming the SAX-7 pattern in the epidermis is not fully understood. Here, we report that the dynein light intermediate chain DLI-1 and the fusogen EFF-1 are required in epidermal cells to pattern SAX-7. While previous reports suggest that these two molecules act cell-autonomously in the PVD, our results show that the disorganized PVD dendritic arbors in these mutants are due to the abnormal SAX-7 localization patterns in epidermal cells. Three lines of evidence support this notion. First, the epidermal SAX-7 pattern was severely affected in dli-1 and eff-1 mutants. Second, the abnormal SAX-7 pattern was predictive of the ectopic PVD dendrites. Third, expression of DLI-1 or EFF-1 in the epidermis rescued both the SAX-7 pattern and the disorganized PVD dendrite phenotypes, whereas expression of these molecules in the PVD did not. We also show that DLI-1 functions cell-autonomously in the PVD to promote distal branch formation. These results demonstrate the unexpected roles of DLI-1 and EFF-1 in the epidermis in the control of PVD dendrite morphogenesis.

Keywords: C. elegans; DLI-1; Dendrite branching; EFF-1; PVD; SAX-7.

MeSH terms

  • Animals
  • Caenorhabditis elegans / metabolism
  • Caenorhabditis elegans Proteins / metabolism*
  • Dendrites / metabolism*
  • Dendrites / pathology
  • Dyneins / metabolism*
  • Membrane Glycoproteins / metabolism*
  • Neural Cell Adhesion Molecules / metabolism*
  • Neurogenesis / physiology
  • Neuronal Plasticity / physiology
  • Phenotype
  • Sensory Receptor Cells / metabolism

Substances

  • Caenorhabditis elegans Proteins
  • EFF-1 protein, C elegans
  • Membrane Glycoproteins
  • Neural Cell Adhesion Molecules
  • SAX-7 protein, C elegans
  • Dyneins