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J Leukoc Biol. 2015 Feb;97(2):297-306. doi: 10.1189/jlb.2A0114-016R. Epub 2014 Nov 25.

Lipid raft-associated β-adducin is required for PSGL-1-mediated neutrophil rolling on P-selectin.

Author information

1
*Institute of Genetics and Cytology, Northeast Normal University, Changchun, China; Department of Bioscience, Changchun Normal University, Changchun, China; and Department of Pathophysiology, Southern Medical University, Guangzhou, China.
2
*Institute of Genetics and Cytology, Northeast Normal University, Changchun, China; Department of Bioscience, Changchun Normal University, Changchun, China; and Department of Pathophysiology, Southern Medical University, Guangzhou, China zengx779@nenu.edu.cn wangxiaoguang58@sina.com.

Abstract

Lipid rafts, a liquid-ordered plasma membrane microdomain, are related to cell-surface receptor function. PSGL-1, a major surface receptor protein for leukocyte, also acts as a signaling receptor in leukocyte rolling. To investigate the role of lipid raft in PSGL-1 signaling in human neutrophils, we quantitatively analyzed lipid raft proteome of human promyelocytic leukemia cell line HL-60 cells and identified a lipid raft-associated protein β-adducin. PSGL-1 ligation induced dissociation of the raft-associated protein β-adducin from lipid rafts and actin, as well as phosphorylation of β-adducin, indicating a transient uncoupling of lipid rafts from the actin cytoskeleton. Knockdown of β-adducin greatly attenuated HL-60 cells rolling on P-selectin. We also showed that Src kinase is crucial for PSGL-1 ligation-induced β-adducin phosphorylation and relocation. Taken together, these results show that β-adducin is a pivotal lipid raft-associated protein in PSGL-1-mediated neutrophil rolling on P-selectin.

KEYWORDS:

LC-MS/MS; Src kinase; phosphorylation; polarization

PMID:
25425738
DOI:
10.1189/jlb.2A0114-016R
[Indexed for MEDLINE]

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