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Phosphorylation of p57/coronin‐1 regulates its binding to actin cytoskeleton
Author(s) -
Oku Teruaki,
Nakano Mai,
Kaneko Yutaka,
Tsuiji Makoto,
Toyoshima Satoshi,
Tsuji Tsutomu
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.763.1
Subject(s) - phosphorylation , microbiology and biotechnology , actin , cytoskeleton , phagosome , biology , actin cytoskeleton , protein kinase c , actin binding protein , phagocytosis , biochemistry , cell
The actin‐binding protein p57/coronin‐1, a member of the coronin protein family, is selectively expressed in hematopoietic cells and plays a crucial role in the immune response through reorganization of actin filaments. We previously reported that p57/coronin‐1 and F‐actin transiently accumulated in phagocytic cups and phagosomal membranes during phagocytosis in neutrophils and neutrophil‐like HL60 cells, and dissociated from phagosomes accompanied by phosphorylation of p57/coronin‐1. In this study, we analyzed phosphorylation sites of p57/coronin‐1 and possible involvement of phosphorylation of p57/coronin‐1 in its binding to F‐actin. Analyses by two‐dimensional gel electrophoresis, MALDI‐TOF‐MS and site‐directed mutagenesis indicated that p57/coronin‐1 had two major phosphorylation sites. The phosphorylation was found to be inhibited by chelerythrine, an inhibitor of protein kinase C (PKC). We also found that phosphorylation of p57/coronin‐1 decreased its binding affinity to F‐actin. These results suggest that the phosphorylation of p57/coronin‐1 by PKC regulates the association of p57/coronin‐1 with actin cytoskeleton and that the regulation is implicated in phagosome maturation.