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The Src family kinases, Fgr, Fyn, Lck, and Lyn, colocalize with coated
membranes in platelets
PE Stenberg, TI Pestina, RJ Barrie and CW Jackson
Department of Pathology, Oregon Health Sciences University, Portland 97201,
USA.
Nonreceptor protein tyrosine kinases phosphorylate proteins, thereby
activating many intracellular signaling pathways and mediating protein-
protein interactions. Protein phosphorylation is regulated in large part by
the subcellular localization of these kinases and their respective
substrates. Src is the most studied of these kinases, although other
members of the Src family have been shown to be important in the
differentiation of specific cell types. Src and Src family members are
reported to be membrane-associated, but detergent- extraction studies have
demonstrated a major difference in the solubility of Src compared with
other members of the Src family (Fgr, Fyn, Lck, Lyn, and Yes), suggesting
that their subcellular distributions may be different. By immunoelectron
microscopy, we demonstrate that, unlike Src, the Src-related kinases are
associated with electron-dense cytoplasmic domains and plasma membrane
domains that correspond in size and frequency to endocytotic vesicles and
coated pits. Clusters of labeling for these kinases also were seen adjacent
to granule membranes. These kinases colocalize with the coated vesicle
protein, clathrin, confirming their association with this class of
endocytotic vesicle. We hypothesize that this vesicular association of
Src-related kinases indicates a role for them in the endocytotic
vesicle-mediated uptake and trafficking of plasma proteins into platelet
granules.
Volume 89,
Issue 7,
pp. 2384-2393,
04/01/1997
Copyright © 1997 by The American Society of Hematology
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