Cargo-sorting signals promote polymerization of adaptor protein-1 in an Arf-1·GTP-independent manner

Intaek Lee, Matthew T. Drake, Linton M. Traub, Stuart Kornfeld

Research output: Contribution to journalArticlepeer-review

7 Scopus citations


Adaptor protein-1 (AP-1) is recruited onto the trans-Golgi network via binding to Arf-1·GTP, cargo-sorting signals and phosphoinositides, where it orchestrates the assembly of clathrin-coated vesicular carriers that transport cargo molecules to endosomes. Here we show that cytosolic AP-1 polymerizes when recruited onto enriched Golgi membranes and liposomes containing covalently attached cargo-sorting signal peptides. Incubation of cytosolic or purified AP-1 with soluble sorting signal peptides also resulted in AP-1 polymerization, showing that Arf-1·GTP and membranes are not required for this process. We propose that cargo-induced polymerization of AP-1 contributes to stabilization of the coat complex in the formation of clathrin-coated buds.

Original languageEnglish
Pages (from-to)63-68
Number of pages6
JournalArchives of Biochemistry and Biophysics
Issue number1
StatePublished - Nov 1 2008


  • Adaptor protein-1
  • Arf-1
  • Cargo-sorting signals
  • Di-leucine-sorting signals
  • Golgi
  • Peptidoliposomes
  • Polymerization
  • Tyrosine-sorting signals


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