Cysteine-rich Region of Raf-1 Interacts with Activator Domain of Post-translationally Modified Ha-Ras (∗)
In: Journal of Biological Chemistry, Jg. 270 (1995-12-22), Heft 51, S. 30274-30277
Online
serialPeriodical
Zugriff:
The interaction between “switch I/effector domain” of Ha-Ras and the Ras-binding domain (RBD, amino acid 51-131) of Raf-1 is essential for signal transduction. However, the importance of the “activator domain” (approximately corresponding to amino acids 26-28 and 40-49) of Ha-Ras and of the “cysteine-rich region” (CRR, amino acids 152-184) of Raf-1 have also been proposed. Here, we found that Raf-1 CRR interacts directly with Ha-Ras independently of RBD and that participation of CRR is necessary for efficient Ras-Raf binding. Furthermore, Ha-Ras carrying mutations (N26G and V45E) in the activator domain failed to bind CRR, whereas they bound RBD normally. On the contrary, Ha-Ras carrying mutations in the switch I/effector domain exhibited severely reduced ability to bind RBD, whereas their ability to bind CRR was unaffected. Mutants that bound to either RBD or CRR alone failed to activate Raf-1. Ha-Ras without post-translational modifications, which lacks the ability to activate Raf-1, selectively lost the ability to bind CRR. These results suggest that the activator domain of Ha-Ras participates in activation of Raf-1 through interaction with CRR and that post-translational modifications of Ha-Ras are required for this interaction.
Titel: |
Cysteine-rich Region of Raf-1 Interacts with Activator Domain of Post-translationally Modified Ha-Ras (∗)
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Autor/in / Beteiligte Person: | Hu, Chang-Deng ; Kariya, Ken-ichi ; Tamada, Masako ; Akasaka, Kazuhito ; Shirouzu, Mikako ; Yokoyama, Shigeyuki ; Kataoka, Tohru |
Link: | |
Zeitschrift: | Journal of Biological Chemistry, Jg. 270 (1995-12-22), Heft 51, S. 30274-30277 |
Veröffentlichung: | 1995 |
Medientyp: | serialPeriodical |
ISSN: | 0021-9258 (print) ; 1083-351X (print) |
DOI: | 10.1074/jbc.270.51.30274 |
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