1995
DOI: 10.1128/mcb.15.12.6746
|View full text |Cite
|
Sign up to set email alerts
|

Identification of Rap1 as a Target for the Crk SH3 Domain-Binding Guanine Nucleotide-Releasing Factor C3G

Abstract: Protein-protein interaction plays important roles in transducing signals elicited from receptors on the cell surface to the nucleus. The Src homology 2 (SH2) and SH3 domains have been shown to bind to tyrosine-phosphorylated proteins (33) and proline-rich motifs (54), respectively (reviewed in references 4, 27, 51, and 61). There are a number of signaling molecules involved in the tyrosine kinase cascade which have either the SH2 domain or the SH3 domain or both, including the GTPase-activating protein for Ras… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
2
1

Citation Types

15
317
3
3

Year Published

1997
1997
2024
2024

Publication Types

Select...
6
1

Relationship

0
7

Authors

Journals

citations
Cited by 355 publications
(338 citation statements)
references
References 67 publications
15
317
3
3
Order By: Relevance
“…These ®ndings suggest that Rap2 proteins most likely have their own regulatory proteins and their identification might help elucidating the biological function of Rap2. We con®rm the results of Gotoh et al (1995) that C3G does not stimulate the guanine nucleotide dissociation from H-and N-Ras ( Figure 3; Table 1), but we now extend this ®nding to K-Ras (Table 1), Rras (3.6-fold stimulation by 1 mM C3G-CD) and TC21 (4.0-fold stimulation by 1 mM C3G-CD). Bud1 (Rsr1) is believed to be the yeast S. cerevisiae homologue of Rap1 (Bender and Pringle, 1989) and shares some functional homology with Rap1 (McCabe et al, 1992).…”
Section: Resultssupporting
confidence: 85%
See 2 more Smart Citations
“…These ®ndings suggest that Rap2 proteins most likely have their own regulatory proteins and their identification might help elucidating the biological function of Rap2. We con®rm the results of Gotoh et al (1995) that C3G does not stimulate the guanine nucleotide dissociation from H-and N-Ras ( Figure 3; Table 1), but we now extend this ®nding to K-Ras (Table 1), Rras (3.6-fold stimulation by 1 mM C3G-CD) and TC21 (4.0-fold stimulation by 1 mM C3G-CD). Bud1 (Rsr1) is believed to be the yeast S. cerevisiae homologue of Rap1 (Bender and Pringle, 1989) and shares some functional homology with Rap1 (McCabe et al, 1992).…”
Section: Resultssupporting
confidence: 85%
“…In a ®rst attempt to obtain the catalytic domain of C3G, a similar construct (residues 775 ± 1078 in pGEX4T2) to the one described by Gotoh et al (1995) was made. However, in our hands, this GSTfusion protein was highly insoluble (Figure 1) and did not show any guanine nucleotide exchange activity towards Rap1A.…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…In contrast, C3G is an activator of Rap1, which is another Ras-family protein (Gotoh et al, 1995). Overexpression of C3G in NIH3T3 cells cotransfected with activated Ras had a reverting e ect on Rasmediated transformation, suggesting that Rap1 may act as a suppressor of Ras (Gotoh et al, 1995). Additionally, Crk has recently been shown to activate c-Jun kinase (JNK1) through C3G (Tanaka et al, 1997), suggesting that Crk could potentially contribute to the activation of parallel signaling pathways.…”
Section: Discussionmentioning
confidence: 98%
“…Sos is an exchange factor for Ras which results in activation of the mitogen activated protein kinase (MAPK) pathway and Crk has been shown to be essential for positive activation of Ras (Tanaka et al, 1993). In contrast, C3G is an activator of Rap1, which is another Ras-family protein (Gotoh et al, 1995). Overexpression of C3G in NIH3T3 cells cotransfected with activated Ras had a reverting e ect on Rasmediated transformation, suggesting that Rap1 may act as a suppressor of Ras (Gotoh et al, 1995).…”
Section: Discussionmentioning
confidence: 99%