LST1/A is a myeloid leukocyte-specific transmembrane adaptor protein recruiting protein tyrosine phosphatases SHP-1 and SHP-2 to the plasma membrane |
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Authors: | Draber Peter Stepanek Ondrej Hrdinka Matous Drobek Ales Chmatal Lukas Mala Linda Ormsby Tereza Angelisova Pavla Horejsi Vaclav Brdicka Tomas |
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Affiliation: | Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, 142 20 Prague, Czech Republic. |
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Abstract: | Transmembrane adaptor proteins are membrane-anchored proteins consisting of a short extracellular part, a transmembrane domain, and a cytoplasmic part with various protein-protein interaction motifs but lacking any enzymatic activity. They participate in the regulation of various signaling pathways by recruiting other proteins to the proximity of cellular membranes where the signaling is often initiated and propagated. In this work, we show that LST1/A, an incompletely characterized protein encoded by MHCIII locus, is a palmitoylated transmembrane adaptor protein. It is expressed specifically in leukocytes of the myeloid lineage, where it localizes to the tetraspanin-enriched microdomains. In addition, it binds SHP-1 and SHP-2 phosphatases in a phosphotyrosine-dependent manner, facilitating their recruitment to the plasma membrane. These data suggest a role for LST1/A in negative regulation of signal propagation. |
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Keywords: | Adaptor Proteins Major Histocompatibility Complex (MHC) Myeloid Cell Signal Transduction Tetraspanins LST1 SHP-1 SHP-2 |
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