The authors found that a sequence containing the amino acid motif NPFX(1,2)D, previously characterized as an endocytic targeting signal in yeast, is sufficient to direct the uptake of a truncated cell surface receptor. A two-hybrid screen for NPFX(1,2)D-binding proteins yielded Sla1p, which is known to interact with the endocytic machinery and regulate actin dynamics. Disrupting Sla1p expression inhibited NPFX(1,2)D-mediated endocytosis.
Combined with previous findings, the results imply that Sla1p is part of...
The Rockefeller University Press
2002
The Rockefeller University Press
2002
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