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Vol. 12, Issue 11, 3550-3562, November 2001
and
Department of Biochemistry, Weill Medical College of Cornell
University, New York, New York 10021
On treatment with chemoattractant, the neutrophil plasma membrane
becomes organized into detergent-resistant membrane domains (DRMs), the
distribution of which is intimately correlated with cell polarization.
Plasma membrane at the front of polarized cells is susceptible to
extraction by cold Triton X-100, whereas membrane at the rear is
resistant to extraction. After cold Triton X-100 extraction, DRM
components, including the transmembrane proteins CD44 and CD43, the
GPI-linked CD16, and the lipid analog, DiIC16, are retained
within uropods and cell bodies. Furthermore, CD44 and CD43 interact
concomitantly with DRMs and with the F-actin cytoskeleton, suggesting a
mechanism for the formation and stabilization of DRMs. By tracking the
distribution of DRMs during polarization, we demonstrate that DRMs
progress from a uniform distribution in unstimulated cells to small,
discrete patches immediately after activation. Within 1 min, DRMs form
a large cap comprising the cell body and uropod. This process is
dependent on myosin in that an inhibitor of myosin light chain kinase
can arrest DRM reorganization and cell polarization. Colabeling DRMs
and F-actin revealed a correlation between DRM distribution and F-actin
remodeling, suggesting that plasma membrane organization may orient
signaling events that control cytoskeletal rearrangements and,
consequently, cell polarity.
Corresponding authors. E-mail
addresses: frmaxie{at}med.cornell.edu or lpierini{at}med.cornell.edu.
*
Present address: Département de Bactériologie et de
Mycologie, Unité des Interactions Bactéries-Cellules.
Institut Pasteur, France; e-mail: sseveau{at}pasteur.fr.
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