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RIIb in B Cells1
Departments of
*
Microbiology and
Internal Medicine, Ohio State University, OH 43210; and
Affinity Sensors, Franklin, MA 02038
Our recent studies revealed that the inositol phosphatase Src
homology 2 (SH2) domain-containing inositol phosphatase (SHIP) is
phosphorylated and associated with Shc exclusively under negative
signaling conditions in B cells, which is due to recruitment of the
SHIP SH2 domain to the Fc
RIIb. In addition, we reported that
SHIP-Shc interaction involves both SHIP SH2 and Shc phosphotyrosine
binding domains. These findings reveal a paradox in which the single
SH2 domain of SHIP is simultaneously engaged to two different proteins:
Shc and FcRIIb. To resolve this paradox, we examined the protein
interactions of SHIP. Our results demonstrated that isolated FcRIIb
contains SHIP but not Shc; likewise, Shc isolates contain SHIP but not
FcRIIb. In contrast, SHIP isolates contain both proteins, revealing
two separate pools of SHIP: one bound to FcRIIb and one bound to
Shc. Kinetic studies reveal rapid SHIP association with FcRIIb but
slower and more transient association with Shc. Affinity measurements
using a recombinant SHIP SH2 domain and phosphopeptides derived from
FcRIIb (corresponding to Y273) and Shc (corresponding to Y317)
revealed an approximately equal rate of binding but a 10-fold faster
dissociation rate for FcRIIb compared with Shc phosphopeptide and
yielding in an affinity of 2.1 µM for FcRIIb and 0.26 µM for
Shc. These findings are consistent with a model in which SHIP
transiently associates with FcRIIb to promote SHIP phosphorylation,
whereupon SHIP binds to Shc and dissociates from
FcRIIb.
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