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LST1/A is a myeloid leukocyte-specific transmembrane adaptor protein recruiting protein tyrosine phosphatases SHP-1 and SHP-2 to the plasma membrane.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 2012 Jun 29; Vol. 287 (27), pp. 22812-21. Date of Electronic Publication: 2012 May 15. - Publication Year :
- 2012
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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.
- Subjects :
- Amino Acid Sequence
HEK293 Cells
HeLa Cells
Humans
Intracellular Signaling Peptides and Proteins
Jurkat Cells
Major Histocompatibility Complex physiology
Membrane Proteins chemistry
Membrane Proteins genetics
Molecular Sequence Data
Myeloid Cells cytology
Plakins metabolism
Primary Cell Culture
Protein Structure, Tertiary physiology
Protein Transport physiology
Pseudopodia metabolism
Signal Transduction physiology
U937 Cells
Cell Membrane metabolism
Membrane Proteins metabolism
Myeloid Cells metabolism
Protein Tyrosine Phosphatase, Non-Receptor Type 11 metabolism
Protein Tyrosine Phosphatase, Non-Receptor Type 6 metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1083-351X
- Volume :
- 287
- Issue :
- 27
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 22589543
- Full Text :
- https://doi.org/10.1074/jbc.M112.339143