AP-2-containing clathrin coats assemble on mature lysosomes

Linton M. Traub, Sergei I. Bannykh, Jill E. Rodel, Meir Aridor, William E. Balch, Stuart Kornfeld

Research output: Contribution to journalArticlepeer-review

101 Scopus citations


Coat proteins appear to play a general role in intracellular protein trafficking by coordinating a membrane budding event with cargo selection. Here we show that the AP-2 adaptor, a clathrin-associated coat-protein complex that nucleates clathrin-coated vesicle formation at the cell surface, can also initiate the assembly of normal polyhedral clathrin coats on dense lysosomes under physiological conditions in vitro. Clathrin coal formation on lysosomes is temperature dependent, displays an absolute requirement for ATP, and occurs in both semi-intact cells and on purified lysosomes, suggesting that clathrin-coated vesicles might regulate retrograde membrane traffic out of the lysosomal compartment.

Original languageEnglish
Pages (from-to)1801-1814
Number of pages14
JournalJournal of Cell Biology
Issue number6 II
StatePublished - 1996


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