The Aplastic Anemia and MDS International Foundation (AAMDSIF) has awarded Isabel Merida's study on the role of diacylglycerol kinase zeta in early stages of aplastic anemia with a two-year grant.
AAMDSIF is the world's leading nonprofit health organization dedicated to patients afflicted with bone marrow failure disease. For nearly 30 years, AAMDSIF has provided research grants totaling in excess of $4 million to an international group of more than 75 researchers to help advance the understanding and treatment of aplastic anemia, myelodysplastic syndromes (MDS), and paroxysmal nocturnal hemoglobinuria (PNH).
The Álvaro Entrecanales Foundation and the Jerôme Lejeune Foundation have awarded Cristina Rodríguez from the Isabel Mérida group at the CNB the predoctoral fellowship in basic and clinical research in Down Syndrome, Trisonomy 21.
Cell Signal. 2014;. pii: S0898-6568(14)00227-7.
Bartolomé RA, Díaz-Martínez M, Coló GP, Arellano-Sánchez N, Torres-Ayuso P, Kleinovink JW, Mérida I, Teixidó J.
Activation of the GTPase RhoA linked to cell invasion can be tightly regulated following Gα13 stimulation. We have used a cellular model displaying Gα13-dependent inhibition of RhoA activation associated with defective cell invasion to the chemokine CXCL12 to characterize the molecular players regulating these processes.
Using both RNAi transfection approaches and protein overexpression experiments here we show that the Src kinase Blk is involved in Gα13-activated tyrosine phosphorylation of p190RhoGAP, which causes RhoA inactivation and ultimately leads to deficient cell invasion. Characterization of molecular interplays between Gα13, Blk and p190RhoGAP revealed that Blk binds Gα13, and that Blk-mediated p190RhoGAP phosphorylation upon Gα13 activation correlates with weakening of Gα13-Blk association connected to increased Blk-p190RhoGAP assembly.
These results place Blk upstream of the p190RhoGAP-RhoA pathway in Gα13-activated cells, overall representing an opposing signaling module during CXCL12-triggered invasion. In addition, analyses with Blk- or Gα13-knockdown cells indicated that Blk can also mediate CXCL12-triggered phosphorylation of p190RhoGAP independently of Gα13. However, even if CXCL12 induces the Blk-mediated GAP phosphorylation, the simultaneous stimulation of the guanine-nucleotide exchange factor Vav1 by the chemokine, as earlier reported, leads to a net increase in RhoA activation. Therefore, when Gα13 is concurrently stimulated with CXCL12 there appears to be sufficient Blk activity to promote adequate levels of p190RhoGAP tyrosine phosphorylation to inactivate RhoA and to impair cell invasiveness.
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