FERM domain of moesin desorbs the basic-rich cytoplasmic domain of l-selectin from the anionic membrane surface.
FERM domain of moesin desorbs the basic-rich cytoplasmic domain of l-selectin from the anionic membrane surface.
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DOI:
10.1016/j.jmb.2013.06.008
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发表时间:
2013-09-23
影响因子:
5.6
通讯作者:
Li, Renhao
中科院分区:
文献类型:
--
作者:
Deng, Wei;Cho, Sungyun;Li, Renhao
Moesin and calmodulin (CaM) jointly associate with the cytoplasmic domain of l-selectin in the cell to modulate the function and ectodomain shedding of l-selectin. Using fluorescence spectroscopy, we have examined the association of moesin FERM domain with the recombinant transmembrane and cytoplasmic domains of l-selectin (CLS) reconstituted in model phospholipid liposomes. The dissociation constant of moesin FERM domain to CLS in the phosphatidylcholine liposome is about 300 nM. In contrast to disrupting the CaM association with CLS, inclusion of anionic phosphatidylserine lipids in the phosphatidylcholine liposome increased the apparent binding affinity of moesin FERM domain for CLS. Using the environmentally sensitive fluorescent probe attached to the cytoplasmic domain of CLS and the nitroxide quencher attached to the lipid bilayer, we showed that the association of moesin FERM domain induced the desorption of the basic-rich cytoplasmic domain of CLS from the anionic membrane surface, which enabled subsequent association of CaM to the cytoplasmic domain of CLS. These results have elucidated the molecular basis for the moesin/l-selectin/CaM ternary complex and suggested an important role of phospholipids in modulating l-selectin function and shedding.
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DOI:
10.1074/jbc.m806983200
发表时间:
2009-03-27
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
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影响因子:
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发表时间:
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影响因子:
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10.1073/pnas.95.4.1556
发表时间:
1998-02-17
影响因子:
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影响因子:
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