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Engagement of CD99 triggers the exocytic transport of ganglioside GM1 and the reorganization of actin cytoskeleton
Author(s) -
Yoon Sang Soon,
Jung Kyung In,
Choi Yoon-La,
Choi Eun Young,
Lee Im-Soon,
Park Seong Hoe,
Kim Tae Jin
Publication year - 2003
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/s0014-5793(03)00268-0
Subject(s) - microbiology and biotechnology , cytoskeleton , actin cytoskeleton , lipid raft , cytochalasin d , actin , vesicular transport protein , immunological synapse , chemistry , biology , signal transduction , cell , vesicle , biochemistry , membrane , t cell , genetics , t cell receptor , immune system
We studied the role of lipid rafts and actin cytoskeleton in CD99‐mediated signaling to elucidate the mechanism of protein transport upon CD99 engagement. CD99 engagement in Jurkat cells elicited the exocytic transport of GM1 as well as several surface molecules closely related with CD99 functions. In addition, CD99 molecules were rapidly incorporated into lipid rafts and appeared to rearrange the actin cytoskeleton upon CD99 stimulation. Association of CD99 with actin cytoskeleton was inhibited by methyl‐β‐cyclodextrin, while CD99‐mediated GM1 clustering was inhibited by cytochalasin D. Therefore, we suggest that CD99 may play a role in the vesicular transport of transmembrane proteins and lipid rafts from the intracellular location to the cell surface, possibly by effecting actin cytoskeleton reorganization.