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Vol. 11, Issue 8, 2743-2756, August 2000
and
*Department of Biology, Yonsei University, Seoul, Korea 120-749;
and In the nematode Caenorhabditis elegans, there exist
two µ1 medium chains of the AP-1 clathrin-associated protein complex. Mutations of unc-101, the gene that encodes one of the
µ1 chains, cause pleiotropic effects (Lee et al.,
1994). In this report, we identified and analyzed the second µ1 chain
gene, apm-1. Unlike the mammalian homologs, the two
medium chains are expressed ubiquitously throughout development. RNA
interference (RNAi) experiments with apm-1 showed that
apm-1 and unc-101 were redundant in
embryogenesis and in vulval development. Consistent with this, a hybrid
protein containing APM-1, when overexpressed, rescued the phenotype of an unc-101 mutant. However, single disruptions of
apm-1 or unc-101 have distinct
phenotypes, indicating that the two medium chains may have distinct
functions. RNAi of any one of the small or large chains of AP-1 complex
(HHMI and Division of Biology, Caltech, California
91125
1, 
1, or 
) showed a phenotype identical to that caused by the
simultaneous disruption of unc-101 and
apm-1, but not that by single disruption of either gene.
This suggests that the two medium chains may share large and small
chains in the AP-1 complexes. Thus, apm-1 and
unc-101 encode two highly related µ1 chains that share
redundant and distinct functions within AP-1 clathrin-associated
protein complexes of the same tissue.
Corresponding author. E-mail address:
leej{at}yonsei.ac.kr.
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