Palmitoylated transmembrane adaptor proteins in leukocyte signaling.
Transmembrane adaptor proteins (TRAPs) are structurally related proteins that have no enzymatic function, but enable inducible recruitment of effector molecules to the plasma membrane, usually in a phosphorylation dependent manner. Numerous surface receptors employ TRAPs for either propagation or negative regulation of the signal transduction. Several TRAPs (LAT, NTAL, PAG, LIME, PRR7, SCIMP, LST1/A, and putatively GAPT) are known to be palmitoylated that could facilitate their localization in lipid rafts or tetraspanin enriched microdomains. This review summarizes expression patterns, binding partners, signaling pathways, and biological functions of particular palmitoylated TRAPs with an emphasis on the three most recently discovered members, PRR7, SCIMP, and LST1/A. Moreover, we discuss in silico methodology used for discovery of new family members, nature of their binding partners, and microdomain localization.
Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Prague, Czech Republic.
Ondrej
O
Stepanek
Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Prague, Czech Republic.
Peter
P
Draber
Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Prague, Czech Republic. Electronic address: vaclav.horejsi@img.cas.cz.
Vaclav
V
Horejsi
D048868:Adaptor Proteins, Signal Transducing / Q000378:metabolism*; D006801:Humans; D007962:Leukocytes / Q000378:metabolism / Q000502:physiology*; D054878:Lipoylation; D021962:Membrane Microdomains / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism*; D015398:Signal Transduction
D048868:Adaptor Proteins, Signal Transducing; D008565:Membrane Proteins
Adaptor; LAT; LST1; PRR7; Palmitoylation; SCIMP