التفاصيل البيبلوغرافية
| العنوان: |
The Function of Embryonic Stem Cell-expressed RAS (E-RAS), a Unique RAS Family Member, Correlates with Its Additional Motifs and Its Structural Properties. |
| المؤلفون: |
Nakhaei-Rad, Saeideh1, Nakhaeizadeh, Hossein1, Kordes, Claus2, Cirstea, Ion C.1,3, Schmick, Malte4, Dvorsky, Radovan1, Bastiaens, Philippe I. H.4, Häussinger, Dieter2, Ahmadian, Mohammad Reza1 reza.ahmadian@uniduesseldorf.de |
| المصدر: |
Journal of Biological Chemistry. 6/19/2015, Vol. 290 Issue 25, p15892-15903. 12p. |
| مصطلحات موضوعية: |
*EMBRYONIC stem cell research, *LIVER cells, *BINDING sites, *TRYPTOPHAN, *CYTOSKELETAL proteins |
| مستخلص: |
E-RAS is a member of the RAS family specifically expressed in embryonic stem cells, gastric tumors, and hepatic stellate cells. Unlike classical RAS isoforms (H-, N-, and K-RAS4B), E-RAS has, in addition to striking and remarkable sequence deviations, an extended 38-amino acid-long unique N-terminal region with still unknown functions. We investigated the molecular mechanism of E-RAS regulation and function with respect to its sequence and structural features. We found that N-terminal extension of E-RAS is important for E-RAS signaling activity. E-RAS protein most remarkably revealed a different mode of effector interaction as compared with H-RAS, which correlates with deviations in the effector-binding site of E-RAS. Of all these residues, tryptophan 79 (arginine 41 in H-RAS), in the interswitch region, modulates the effector selectivity of RAS proteins from H-RAS to E-RAS features. [ABSTRACT FROM AUTHOR] |
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