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(Received for publication, September 18, 1996, and in revised form, November 1, 1996)
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,
and
From the In intact cells, mitogen-activated
protein kinase-activated protein (MAPKAP) kinase 2 is rapidly activated
by various cytokines, stresses, and chemotactic factors. The small heat
shock protein p27 has been shown to be a substrate for MAPKAP kinase 2. Recently, we identified a novel substrate, designated p60, for MAPKAP
kinase 2 in human neutrophils (Zu, Y.-L., Ai, Y., Gilchrist, A.,
Labadia, M. E., Sha'afi, R. I., and Huang, C.-K. (1996) Blood
87, 5287-5296). To further understand the signaling pathway of
MAPKAP kinase 2, we have purified p60 from a heat-treated neutrophil
lysate by DEAE-cellulose chromatography and SDS-polyacrylamide gel
electrophoresis. Microsequencing of five peptides derived from purified
p60 indicates that p60 is lymphocyte-specific protein 1 (LSP1).
Furthermore antibodies specific for human and mouse LSP1 react with
human and mouse p60. The sequence of human LSP1 indicates two serine residues at positions 204 and 252 as potential phosphorylation sites.
The amino acid sequences surrounding these two sites are in agreement
with the consensus sequence (Xaa-Xaa-Hyd-Xaa-Arg-Xaa-Xaa-Ser-Xaa-Xaa) for phosphorylation by MAPKAP kinase 2. Both serine residues in human
LSP1 and the corresponding conserved serine residues in mouse LSP1 are
in the basic C-terminal F-actin binding domain. Various fusion proteins
of wild type and truncated mouse LSP1 with glutathione
S-transferase were tested for their capacity to be
phosphorylated by MAPKAP kinase 2. The results indicate that LSP1 is a
substrate for MAPKAP kinase 2 in vitro and that the
phosphorylation sites are located in the basic C-terminal domain of
LSP1. Because both the small heat shock proteins and LSP1 are F-actin
binding proteins, these results suggest a role for MAPKAP kinase 2 in
the regulation of cytoskeletal structure or function.
Department of Pathology, University of
Connecticut Health Center, Farmington, Connecticut 06030-3105 and the
¶ Arthritis Centre-Research Unit, The Toronto Hospital Research
Institute and Department of Immunology, University of Toronto, Toronto,
Ontario M5T 2S8, Canada
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