Tyrosine phosphorylation of Dbl regulates GTPase signaling
In: The Journal of biological chemistry, Jg. 289 (2014-04-30), Heft 24
Online
unknown
Zugriff:
Rho GTPases are molecular “switches” that cycle between “on” (GTP-bound) and “off” (GDP-bound) states and regulate numerous cellular activities such as gene expression, protein synthesis, cytoskeletal rearrangements, and metabolic responses. Dysregulation of GTPases is a key feature of many diseases, especially cancers. Guanine nucleotide exchange factors (GEFs) of the Dbl family are activated by mitogenic cell surface receptors and activate the Rho family GTPases Cdc42, Rac1, and RhoA. The molecular mechanisms that regulate GEFs from the Dbl family are poorly understood. Our studies reveal that Dbl is phosphorylated on tyrosine residues upon stimulation by growth factors and that this event is critical for the regulated activation of the GEF. These findings uncover a novel layer of complexity in the physiological regulation of this protein.
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Tyrosine phosphorylation of Dbl regulates GTPase signaling
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Autor/in / Beteiligte Person: | Gupta, Meghana ; Thakur, Varsha ; Manor, Danny ; Qi, Xiaojun |
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Zeitschrift: | The Journal of biological chemistry, Jg. 289 (2014-04-30), Heft 24 |
Veröffentlichung: | 2014 |
Medientyp: | unknown |
ISSN: | 1083-351X (print) |
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