Journal
JOURNAL OF CELL BIOLOGY
Volume 163, Issue 6, Pages 1281-1290Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200307157
Keywords
clathrin; adaptors; coats; endocytosis; endosomes
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The sorting of transmembrane proteins to endosomes and lysosomes is mediated by signals present in the cytosolic tails of the proteins. A subset of these signals conform to the [DE]XXXL[LI] consensus motif and mediate sorting via interactions with heterotetrameric adaptor protein (AP) complexes. However, the identity of the AP subunits that recognize these signals remains controversial. We have used a yeast three-hybrid assay to demonstrate that [DE]XXXL[LI]-type signals from the human immunodeficiency virus negative factor protein and the lysosomal integral membrane protein II interact with comb nations of the gamma and sigma1 subunits of AP-1 and the 8 and sigma3 subunits of AP-3, but not the analogous combinations of AP-2 and AP-4 subunits. The sequence requirements for these interactions are similar to those for binding to the whole AP complexes in vitro and for function of the signals in vivo. These observations reveal a novel mode of recognition of sorting signals involving the gamma/delta and sigma subunits of AP-1 and AP-3.
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