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Vol. 12, Issue 10, 2907-2920, October 2001
Cell Biology and Metabolism Branch, National Institute of
Child Health and Human Development, National Institutes of Health,
Bethesda, Maryland, 20892
Adaptins are subunits of adaptor protein (AP) complexes
involved in the formation of intracellular transport vesicles and in
the selection of cargo for incorporation into the vesicles. In this
article, we report the results of a survey for adaptins from sequenced
genomes including those of man, mouse, the fruit fly Drosophila
melanogaster, the nematode Caenorhabditis
elegans, the plant Arabidopsis thaliana, and the
yeasts, Saccharomyces cerevisiae and
Schizosaccharomyces pombe. We find that humans, mice,
and Arabidopsis thaliana have four AP complexes (AP-1,
AP-2, AP-3, and AP-4), whereas D. melanogaster,
C. elegans, S. cerevisiae, and S.
pombe have only three (AP-1, AP-2, and AP-3). Additional diversification of AP complexes arises from the existence of adaptin isoforms encoded by distinct genes or resulting from alternative splicing of mRNAs. We complete the assignment of adaptins to AP complexes and provide information on the chromosomal localization, exon-intron structure, and pseudogenes for the different adaptins. In
addition, we discuss the structural and evolutionary relationships of
the adaptins and the genetic analyses of their function. Finally, we
extend our survey to adaptin-related proteins such as the GGAs and
stonins, which contain domains homologous to the adaptins.
Online version of this essay contains
supplemental tabular material. Online version is available at
www.molcellbiol.org.
*
Corresponding author: E-mail: juan{at}helix.nih.gov
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