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AP2 hemicomplexes contribute independently to synaptic vesicle endocytosis.

Mingyu Gu | Qiang Liu | Shigeki Watanabe | Lin Sun | Gunther Hollopeter | Barth D Grant | Erik M Jorgensen
eLife | 2013

The clathrin adaptor complex AP2 is thought to be an obligate heterotetramer. We identify null mutations in the α subunit of AP2 in the nematode Caenorhabditis elegans. α-adaptin mutants are viable and the remaining μ2/β hemicomplex retains some function. Conversely, in μ2 mutants, the alpha/sigma2 hemicomplex is localized and is partially functional. α-μ2 double mutants disrupt both halves of the complex and are lethal. The lethality can be rescued by expression of AP2 components in the skin, which allowed us to evaluate the requirement for AP2 subunits at synapses. Mutations in either α or μ2 subunits alone reduce the number of synaptic vesicles by about 30%; however, simultaneous loss of both α and μ2 subunits leads to a 70% reduction in synaptic vesicles and the presence of large vacuoles. These data suggest that AP2 may function as two partially independent hemicomplexes. DOI:http://dx.doi.org/10.7554/eLife.00190.001.

Pubmed ID: 23482940

Research resources used in this publication

None found

Antibodies used in this publication

None found

Associated grants

  • Agency: NIGMS NIH HHS, United States
    Id: R01 GM067237
  • Agency: NINDS NIH HHS, United States
    Id: R01 NS034307
  • Agency: NINDS NIH HHS, United States
    Id: NS034307
  • Agency: NIGMS NIH HHS, United States
    Id: GM067237

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