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A more recent version of this article appeared on November 1, 2003
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Submitted on May 19, 2003
Revised on July 17, 2003
Accepted on July 20, 2003
1 Departments of Pharmaceutical Sciences
2 Physiology and Biophysics
3 Cell and Neurobiology
4 University of Southern California, Los
Angeles, California, USA and Leibniz Institute for
Neurobiology
5 Physiology and
Biophysics and
Ophthalmology
6 Departments of Pharmaceutical Sciences, Physiology and
Biophysics and
Ophthalmology
* Corresponding author. E-mail address: shalvar{at}usc.edu.
Here we investigate the contributions of actin filaments and
accessory proteins to apical clathrin-mediated endocytosis in primary
rabbit lacrimal acini. Confocal fluorescence and electron microscopy
revealed that cytochalasin D promoted apical accumulation of clathrin,
-adaptin, dynamin and F-actin and increased the amounts of coated
pits and vesicles at the apical plasma membrane. Sorbitol density
gradient analysis of membrane compartments showed that cytochalasin D
increased 14C-dextran association with apical membranes
from stimulated acini, consistent with functional inhibition of apical
endocytosis. Recombinant syndapin SH3 domains interacted with lacrimal
acinar dynamin, N-WASP and synaptojanin; their introduction by
electroporation elicited remarkable accumulation of clathrin, accessory
proteins and coated pits at the apical plasma membrane. These SH3
domains also significantly (p 
0.05) increased F-actin, with
substantial colocalization of dynamin and N-WASP with the additional
filaments. Co-electroporation with the VCA domain of N-WASP blocked the
increase in F-actin and reversed the morphological changes indicative
of impaired apical endocytosis. We suggest that transient modulation of
actin polymerization by syndapins through activation of the Arp2/3
complex via N-WASP coordinates dynamin-mediated vesicle fission at the
apical plasma membrane of acinar epithelia. Trapping of assembled
F-actin intermediates during this process by cytochalasin D or syndapin
SH3 domains impairs endocytosis.
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