PMID: 8948442Jun 15, 1995Paper

ADP-ribosylation of the GTP-binding protein RhoA blocks cytoplasmic division in human myelomonocytic cells

The Biochemical Journal
M AepfelbacherP C Weber

Abstract

To test the role of Rho GTP-binding proteins in growth regulation of human myelomonocytic tumour cells we used recombinant C3 exoenzyme of Clostridium botulinum to specifically ADP-ribosylate and inactivate Rho proteins in situ. In homogenates of HL60 cells, the C3 exoenzyme [32P]ADP-ribosylated one protein that was identified as RhoA by immunoblot and two-dimensional gel electrophoresis. [32P]ADP ribosylation of RhoA in HL60 homogenates in vitro was reduced to 10-20% when cells in culture were pretreated with C3 exoenzyme (10 micrograms, 24 h), indicating that 80-90% of RhoA could be ADP-ribosylated in situ. The C3 exoenzyme inhibited HL60 cell proliferation by up to 80% and the degree of growth inhibition correlated with the amount of in situ ADP-ribosylated RhoA in a time- and dose-dependent manner. Cell cycle analysis demonstrated that the C3 exoenzyme-treated HL60 cells accumulated in mitosis, and nuclear staining revealed binucleated cells. These findings suggest that RhoA has a key role in human myelomonocytic tumour cell growth by regulating cytoplasmic division.

Citations

Mar 15, 2000·Protein Science : a Publication of the Protein Society·P W ReadR K Nakamoto
Mar 5, 2016·Science Signaling·Duyen Amy BuiJoan S Brugge
Nov 2, 2002·The Journal of Biological Chemistry·Huifei LiuLola M Reid
Mar 8, 2000·The Journal of Cell Biology·S N ProkopenkoH J Bellen
Feb 3, 2005·The Journal of Biological Chemistry·Arthur S AlbertsJeffrey A Frost

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