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Journal of Cell Science, Vol 114, Issue 7 1357-1366, Copyright © 2001 by Company of Biologists

JOURNAL ARTICLES

Analysis of R-Ras signalling pathways

AJ Self, E Caron, HF Paterson and A Hall
MRC Laboratory for Molecular Cell Biology, CRC Oncogene and Signal Transduction Group and Department of Biochemistry, University College London, Gower Street, London WC1E 6BT, UK. Alan.Hall@ucl.ac.uk

R-Ras has a high degree of sequence homology to Ras and to other members of the Ras subfamily including Rap, TC21 and M-Ras. Activated versions of Ras and TC21 are highly transforming in a variety of cell lines and mutated forms of both proteins have been found in human tumours. R-Ras interacts with many of the same proteins as Ras and TC21, including c-Raf1, and can induce transformed foci, although this activity is weak compared to Ras and appears to be cell-type specific. Here, we have investigated R-Ras signalling pathways in a variety of cell types. We find that microinjection of activated R-Ras into quiescent fibroblasts stimulates cell cycle progression through G(1) phase and subsequent DNA synthesis. However, unlike Ras, R-Ras does not activate the ERK MAP kinase pathway nor does it activate the JNK or p38/Mpk2 MAP kinase pathways. Microinjection of R-Ras into PC12 cells does not induce terminal differentiation, but instead causes extensive cell spreading, consistent with R-Ras having a role in integrin activation. Finally, in a macrophage cell line, R-Ras activates the (&agr;)(M)(&bgr;)(2 )integrin via the small GTPase Rap1, leading to phagocytosis of opsonized red blood cells, whereas Ras does not. These results indicate that R-Ras has an important role in the regulation of cell growth and adhesion, but that this is mediated through downstream signals distinct from those used by Ras.


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© The Company of Biologists Ltd 2001