RRC ID 62170
Author Kumagai H, Oki T, Tamitsu K, Feng SZ, Ono M, Nakajima H, Bao YC, Kawakami Y, Nagayoshi K, Copeland NG, Gilbert DJ, Jenkins NA, Kawakami T, Kitamura T.
Title Identification and characterization of a new pair of immunoglobulin-like receptors LMIR1 and 2 derived from murine bone marrow-derived mast cells.
Journal Biochem Biophys Res Commun
Abstract We have identified and characterized two mouse cDNAs in a mouse antigen-stimulated bone marrow-derived mast cell cDNA library, both of which encode type I transmembrane proteins. The genes were closely mapped in the distal region of mouse chromosome 11 and expressed not only in mast cells but also widely in leukocytes. The extracellular domains of their encoded proteins contain a single variable immunoglobulin (Ig) motif sharing about 90% identity with amino acids, showing that they comprise a pair of molecules and belong to the Ig superfamily. We named these molecules leukocyte mono-Ig-like receptor1 and 2 (LMIR1 and 2). The intracellular domain of LMIR1 contains several immunoreceptor tyrosine-based inhibition motifs (ITIMs). When cross-linked, the intracellular domain was tyrosine phosphorylated and capable of recruiting tyrosine phosphatases, SHP-1 and SHP-2 and inositol polyphosphate 5-phosphatase, SHIP. LMIR2, on the other hand, contains a short cytoplasmic tail and a characteristic transmembrane domain carrying two positively charged amino acids associated with three kinds of immunoreceptor tyrosine-based activation motif (ITAM)-bearing molecules, DAP10, DAP12, and FcRgamma. These findings suggest that a new pair of ITIM/ITAM-bearing receptors, LMIR1 and 2, regulate mast cell-mediated inflammatory responses through yet to be defined ligand(s).
Volume 307(3)
Pages 719-29
Published 2003-8-1
DOI 10.1016/s0006-291x(03)01245-2
PII S0006291X03012452
PMID 12893283
MeSH Amino Acid Sequence Animals Base Sequence Cell Line Chromosome Mapping Cloning, Molecular Hematopoietic Stem Cells / physiology Mast Cells / immunology* Mice Mice, Inbred C57BL Molecular Sequence Data Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases Phosphoric Monoester Hydrolases / metabolism Phosphorylation Protein Structure, Tertiary Protein Tyrosine Phosphatases / metabolism RNA, Messenger / biosynthesis Receptors, Immunologic / chemistry Receptors, Immunologic / genetics* Receptors, Immunologic / metabolism* Tyrosine / metabolism
IF 2.985
Human and Animal Cells 32Dcl3(RCB1538)