Coronin-1 is phosphorylated at Thr-412 by protein kinase Cα in human phagocytic cells.
Biochem Biophys Rep
; 27: 101041, 2021 Sep.
Article
em En
| MEDLINE
| ID: mdl-34189278
ABSTRACT
Coronin-1, a hematopoietic cell-specific actin-binding protein, is thought to be involved in the phagocytic process through its interaction with actin filaments. The dissociation of coronin-1 from phagosomes after its transient accumulation on the phagosome surface is associated with lysosomal fusion. We previously reported that 1) coronin-1 is phosphorylated by protein kinase C (PKC), 2) coronin-1 has two phosphorylation sites, Ser-2 and Thr-412, and 3) Thr-412 of coronin-1 is phosphorylated during phagocytosis. In this study, we examined which PKC isoform is responsible for the phosphorylation of coronin-1 at Thr-412 by using isotype-specific PKC inhibitors and small interfering RNAs (siRNAs). Thr-412 phosphorylation of coronin-1 was suppressed by Gö6976, an inhibitor of PKCα and PKCßI. This phosphorylation was attenuated by siRNA for PKCα, but not by siRNA for PKCß. Furthermore, Thr-412 of coronin-1 was phosphorylated by recombinant PKCα in vitro, but not by recombinant PKCß. We next examined the effects of Gö6976 on the intracellular distribution of coronin-1 in HL60 cells during phagocytosis. The confocal fluorescence microscopic observation showed that coronin-1 was not dissociated from phagosomes in Gö6976-treated cells. These results indicate that phosphorylation of coronin-1 at Thr-412 by PKCα regulates intracellular distribution during phagocytosis.
ATP, adenosine 5'-triphosphate; Actin-binding protein; Coronin-1; HRP, horseradish peroxidase; OpZ, opsonized zymosan; PBS, phosphate-buffered saline; PKC, protein kinase C; PS, phosphatidylserine; Phagocytosis; Phagosome-lysosome fusion; Protein kinase C; SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electrophoresis; siRNA, small interfering RNA
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Ano de publicação:
2021
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Article