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The myeloid expressed EF‐hand proteins display a diverse pattern of lipid raft association
Author(s) -
Nacken Wolfgang,
Sorg Clemens,
Kerkhoff Claus
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.07.024
Subject(s) - lipid raft , sphingolipid , membrane protein , microbiology and biotechnology , biology , raft , membrane , biochemistry , signal transduction , chemistry , organic chemistry , copolymer , polymer
EF‐hand proteins are known to translocate to membranes, suggesting that they are involved in signaling events located in the cell membrane. Many proteins involved in signaling events associate cholesterol rich membrane domains, so called lipid rafts, which serve as platforms for controlled protein–protein interaction. Here, we demonstrate that the myeloid expressed EF‐hand proteins can be distinguished into three classes with respect to their membrane association. Grancalcin, a myeloid expressed penta EF‐hand protein, is constitutively located in lipid rafts. S100A9 (MRP14) and S100A8 (MRP8) are translocated into detergent resistant lipid structures only after calcium activation of the neutrophils. However, the S100A9/A8 membrane association is cholesterol and sphingolipid independent. On the other hand, the association of S100A12 (EN‐RAGE) and S100A6 (calcyclin) with membranes is detergent sensitive. These diverse affinities to lipid structures of the myeloid expressed EF‐hand proteins most likely reflect their different functions in neutrophils.