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Blood, 15 June 2002, Vol. 99, No. 12, pp. 4494-4502
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
Attachment of the PSGL-1 cytoplasmic domain to the actin
cytoskeleton is essential for leukocyte rolling on
P-selectin
Karen R. Snapp,
Christine
E. Heitzig, and
Geoffrey S. Kansas
From the Department of Microbiology/Immunology,
Northwestern University Medical School, Chicago, IL.
P-selectin glycoprotein ligand-1 (PSGL-1) serves as the leukocyte
ligand for P-selectin, and many of the structural features of its
ectodomain required for interactions with P-selectin have been
uncovered. In contrast, the function of the highly conserved PSGL-1
cytoplasmic domain has not been explored. Stable transfectants expressing similar levels of either wild-type PSGL-1 or truncated PSGL-1 in which only 4 cytoplasmic residues were retained (designated PSGL-1 cyto), were analyzed. Transfectants expressing full-length PSGL-1 rolled well on P-selectin. In contrast, rolling was almost completely absent in cells transfected with PSGL-1cyto, even at low
shear. Importantly, cells expressing truncated PSGL-1 were able to bind
soluble P-selectin and to bind COS cells overexpressing P-selectin,
demonstrating that the P-selectin binding site on the PSGL-1cyto
transfectants was intact and was capable of recognizing P-selectin.
Impaired rolling by PSGL-1cyto transfectants was not due to
alterations in subcellular localization because both wild-type and
truncated PSGL-1 had similar surface distributions on K562
transfectants. Treatment of cells expressing native PSGL-1 with actin
cytoskeletal toxins inhibited adhesion in a dose-dependent way. PSGL-1
was associated with the actin cytoskeleton, and this interaction was
greatly impaired in PSGL-1cyto- expressing cells. The PSGL-1
cytoplasmic domain interacted selectively with the ezrin/radixin/moesin
(ERM) protein moesin, but not with other ERM proteins or several other
cytoskeletal linker proteins. Pharmacologic disruption of interactions
between moesin and F-actin in cells expressing PSGL-1 resulted in a
dose-dependent inhibition of rolling on P-selectin. Thus, attachment of
PSGL-1 to the leukocyte cortical cytoskeleton is essential for
leukocyte rolling on P-selectin.
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