Abstract:
:In RAW 264.7 cells, PKC-ε regulates FcγR-mediated phagocytosis. BMDM behave similarly; PKC-ε concentrates at phagosomes and internalization are reduced in PKC-ε⁻/⁻ cells. Two questions were asked: what is the role of PKC-ε? and what domains are necessary for PKC-ε concentration? Function was studied using BMDM and frustrated phagocytosis. On IgG surfaces, PKC-ε⁻/⁻ macrophages spread less than WT. Patch-clamping revealed that the spreading defect is a result of the failure of PKC-ε⁻/⁻ macrophages to add membrane. The defect is specific for FcγR ligation and can be reversed by expression of full-length (but not the isolated RD) PKC-ε in PKC-ε⁻/⁻ BMDM. Thus, PKC-ε function in phagocytosis requires translocation to phagosomes and the catalytic domain. The expression of chimeric PKC molecules in RAW cells identified the εPS as necessary for PKC-ε targeting. When placed into (nonlocalizing) PKC-δ, εPS was sufficient for concentration, albeit to a lesser degree than intact PKC-ε. In contrast, translocation of δ(εPSC1B) resembled that of WT PKC-ε. Thus, εPS and εC1B cooperate for optimal phagosome targeting. Finally, cells expressing εK437W were significantly less phagocytic than their PKC-ε-expressing counterparts, blocked at the pseudopod-extension phase. In summary, we have shown that εPS and εC1B are necessary and sufficient for targeting PKC-ε to phagosomes, where its catalytic activity is required for membrane delivery and pseudopod extension.
journal_name
J Leukoc Bioljournal_title
Journal of leukocyte biologyauthors
Wood TR,Chow RY,Hanes CM,Zhang X,Kashiwagi K,Shirai Y,Trebak M,Loegering DJ,Saito N,Lennartz MRdoi
10.1189/jlb.1212634subject
Has Abstractpub_date
2013-07-01 00:00:00pages
109-22issue
1eissn
0741-5400issn
1938-3673pii
jlb.1212634journal_volume
94pub_type
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