Abstract:
:Eukaryotic plasma membranes assemble actin filaments within seconds of activation of many receptors, especially during chemotaxis. Here, serum or sphingosine-1-phosphate stimulation of J774 and RAW macrophages released ADP within seconds into the extracellular medium, along with an adenylate kinase activity that converted ADP to ATP. ATP then activated the P2X7 receptor (P2X7R) that was necessary for a peak of plasma-membrane actin assembly within 5 to 10 seconds in P2X7R-expressing J774, RAW and primary macrophages. Neither actin assembly nor characteristic P2X7R channel activity was seen in response to ATP in P2X7R-knockout macrophages, as detected by patch-clamp analysis. Since P2X7R has been shown previously to form a macromolecular complex with actin we propose that it is involved in the membrane assembly of actin. Our data reveal a surprisingly rapid and complex relay of signaling and externalization events that precede and control actin assembly induced by sphingosine-1-phosphate. The overall model we present is strongly supported by the data presented in the accompanying paper that focuses on latex bead phagosomes.
journal_name
J Cell Scijournal_title
Journal of cell scienceauthors
Kuehnel MP,Reiss M,Anand PK,Treede I,Holzer D,Hoffmann E,Klapperstueck M,Steinberg TH,Markwardt F,Griffiths Gdoi
10.1242/jcs.034207subject
Has Abstractpub_date
2009-02-15 00:00:00pages
505-12issue
Pt 4eissn
0021-9533issn
1477-9137pii
jcs.034207journal_volume
122pub_type
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