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Vol. 14, Issue 2, 516-528, February 2003
*Laboratory of Cell Biology, National Heart, Lung, and
Blood Institute, National Institutes of Health, Bethesda, Maryland
20892; and We previously demonstrated, using fluorescence recovery after
photobleaching, that clathrin in clathrin-coated pits at the plasma
membrane exchanges with free clathrin in the cytosol, suggesting that
clathrin-coated pits are dynamic structures. We now investigated whether clathrin at the trans-Golgi network as well as
the clathrin adaptors AP2 and AP1 in clathrin-coated pits at the plasma
membrane and trans-Golgi network, respectively, also
exchange with free proteins in the cytosol. We found that when the
budding of clathrin-coated vesicle is blocked without significantly
affecting the structure of clathrin-coated pits, both clathrin and AP2
at the plasma membrane and clathrin and AP1 at the
trans-Golgi network exchange rapidly with free proteins
in the cytosol. In contrast, when budding of clathrin-coated vesicles
was blocked at the plasma membrane or trans-Golgi
network by hypertonic sucrose or K+ depletion, conditions
that markedly affect the structure of clathrin-coated pits, clathrin
exchange was blocked but AP2 at the plasma membrane and both AP1 and
the GGA1 adaptor at the trans-Golgi network continue to
rapidly exchange. We conclude that clathrin-coated pits are dynamic
structures with rapid exchange of both clathrin and adaptors and that
adaptors are able to exchange independently of clathrin when clathrin
exchange is blocked.
Cell Biology and Metabolism Branch,
National Institute of Child Health and Human Development, National
Institutes of Health, Bethesda, Maryland 20892
Corresponding author. E-mail address:
greenel{at}helix.nih.gov.
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