C. elegans Dynamin mediates the signaling of phagocytic receptor CED-1 for the engulfment and degradation of apoptotic cells

Dev Cell. 2006 Jun;10(6):743-57. doi: 10.1016/j.devcel.2006.04.007.

Abstract

Dynamins are large GTPases that act in multiple vesicular trafficking events. We identified 14 loss-of-function alleles of the C. elegans dynamin gene, dyn-1, that are defective in the removal of apoptotic cells. dyn-1 functions in engulfing cells to control the internalization and degradation of apoptotic cells. dyn-1 acts in the genetic pathway composed of ced-7 (ABC transporter), ced-1 (phagocytic receptor), and ced-6 (CED-1's adaptor). DYN-1 transiently accumulates to the surface of pseudopods in a manner dependent on ced-1, ced-6, and ced-7, but not on ced-5, ced-10, or ced-12. Abnormal vesicle structures accumulate in engulfing cells upon dyn-1 inactivation. dyn-1 and ced-1 mutations block the recruitment of intracellular vesicles to pseudopods and phagosomes. We propose that DYN-1 mediates the signaling of the CED-1 pathway by organizing an intracellular vesicle pool and promoting vesicle delivery to phagocytic cups and phagosomes to support pseudopod extension and apoptotic cell degradation.

Publication types

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

MeSH terms

  • Alleles
  • Amino Acid Sequence
  • Animals
  • Apoptosis*
  • Caenorhabditis elegans / cytology
  • Caenorhabditis elegans / embryology
  • Caenorhabditis elegans / metabolism
  • Caenorhabditis elegans / physiology
  • Caenorhabditis elegans / ultrastructure
  • Caenorhabditis elegans Proteins / metabolism*
  • Conserved Sequence
  • Dynamins / chemistry
  • Dynamins / genetics
  • Dynamins / metabolism*
  • Dynamins / physiology
  • Dynamins / ultrastructure
  • Embryo, Nonmammalian / ultrastructure
  • Helminth Proteins / chemistry
  • Helminth Proteins / genetics
  • Helminth Proteins / metabolism*
  • Helminth Proteins / physiology
  • Helminth Proteins / ultrastructure
  • Membrane Proteins / metabolism*
  • Models, Biological
  • Molecular Sequence Data
  • Mutation
  • Phagocytosis
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid
  • Signal Transduction*

Substances

  • Caenorhabditis elegans Proteins
  • Helminth Proteins
  • Membrane Proteins
  • ced-1 protein, C elegans
  • Dyn-1 protein, C elegans
  • Dynamins