LST1/A is a myeloid leukocyte-specific transmembrane adaptor protein recruiting protein tyrosine phosphatases SHP-1 and SHP-2 to the plasma membrane

0387583 - ÚMG 2013 RIV US eng J - Článek v odborném periodiku
Dráber, Peter - Štěpánek, Ondřej - Hrdinka, Matouš - Drobek, Aleš - Chmátal, Lukáš - Malá, Linda - Ormsby, Tereza - Angelisová, Pavla - Hořejší, Václav - Brdička, Tomáš
LST1/A is a myeloid leukocyte-specific transmembrane adaptor protein recruiting protein tyrosine phosphatases SHP-1 and SHP-2 to the plasma membrane.
Journal of Biological Chemistry. Roč. 287, č. 27 (2012), s. 22812-228221. ISSN 0021-9258. E-ISSN 1083-351X
Grant CEP: GA ČR GEMEM/09/E011; GA ČR(CZ) GBP302/12/G101; GA MŠMT 1M0506
Výzkumný záměr: CEZ:AV0Z50520514
Institucionální podpora: RVO:68378050
Klíčová slova: adaptor proteins * myeloid cell * signal transduction * tetraspanins * LST1/A
Kód oboru RIV: EB - Genetika a molekulární biologie
Impakt faktor: 4.651, rok: 2012

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.
Trvalý link: http://hdl.handle.net/11104/0216734