Format

Send to

Choose Destination
Elife. 2013 Mar 5;2:e00190. doi: 10.7554/eLife.00190.

AP2 hemicomplexes contribute independently to synaptic vesicle endocytosis.

Author information

1
Department of Biology , Howard Hughes Medical Institute, University of Utah , Salt Lake City , United States.

Abstract

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.

KEYWORDS:

AP2; C. elegans; apa-2; apm-2; synaptic vesicle endocytosis

PMID:
23482940
PMCID:
PMC3591783
DOI:
10.7554/eLife.00190
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for eLife Sciences Publications, Ltd Icon for PubMed Central
Loading ...
Support Center