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Differential involvement of H- and K-Ras in Raf-1 activation determines the role of calmodulin in MAPK signaling.

Abstract：

:We have previously demonstrated that inhibition of calmodulin (CaM) and the concomitant reduction of PI3K interfere with H-Ras-mediated activation of Raf-1 [1]. In the present study, we show that CaM has completely opposite effects on K-Ras-mediated Raf-1 activation. The differential contribution of CaM in the regulation of Raf-1 kinase activity via K- or H-Ras correlates with the stimulatory or inhibitory effect of CaM on MAPK phosphorylation depending on the cell type analyzed. FRET microscopy and biochemical analysis show that inhibition of CaM increases K-Ras-GTP levels and consequently its association with Raf-1. Though inhibition of CaM, using the CaM antagonist W-13, significantly increased Raf-1 activation by K-Ras-GTP, MAPK activation downstream K-Ras/Raf-1 was strongly reduced in COS-1 and several other cell lines. In contrast, in other cell lines such as NIH3T3-wt8, W-13-mediated inhibition of CaM increased Raf-1 activity, but resulted in an increase in MAPK phosphorylation. These findings suggest that modulation of K-Ras activity via CaM regulates MAPK signaling only in certain cell types. In support of this hypothesis, the comparison of H- and K-Ras expression, GTP loading and Raf-1 interaction in COS-1 and NIH3T3-wt8 suggests that the overall role of CaM in MAPK signal output is determined by the ratio of activated H- and K-Ras and the cell-specific contribution of each isoform in Raf-1 activation.

journal_name

Cell Signal

journal_title

Cellular signalling

authors

Moretó J,Vidal-Quadras M,Pol A,Santos E,Grewal T,Enrich C,Tebar F

doi

10.1016/j.cellsig.2009.07.018

subject

Has Abstract

pub_date

2009-12-01 00:00:00

pages

1827-36

issue

12

eissn

0898-6568

issn

1873-3913

pii

S0898-6568(09)00225-3

journal_volume

21

pub_type

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