1996
DOI: 10.1073/pnas.93.4.1689
|View full text |Cite
|
Sign up to set email alerts
|

Abstract: (3,4), and two SH2-containing adapter proteins, Grb2 and Shc, have been implicated in its activation. Specifically, these proteins have been shown to bind directly to tyrosine-phosphorylated receptors (5-7) or SH2 docking proteins (such as the insulin receptor substrate 1) (8). Grb2, a 25-kDa protein with two SH3 domains flanking one SH2 domain, shuttles the Ras guanine nucleotide exchange factor, Sosl, to activated receptors (or to insulin receptor substrate 1) (5, 7-11) so that Sosl can activate Ras by catal… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
4
1

Citation Types

14
504
0
2

Year Published

1997
1997
2011
2011

Publication Types

Select...
10

Relationship

0
10

Authors

Journals

citations
Cited by 583 publications
(520 citation statements)
references
References 47 publications
14
504
0
2
Order By: Relevance
“…The APS-associated phosphoproteins were quite similar to those associated with Grb2 and c-Cbl. The major APS binding phosphoprotein, p145 was precipitated with all other antibodies, and it is probably SHIP which is reported to be associated with Shc and Grb2 (Damen et al, 1996;Osborne et al, 1996). A marginal amount of p120 c-Cbl was precipitated with APS.…”
Section: Tyrosine Phosphorylation Of Aps and Its Associated Proteins mentioning
confidence: 92%
“…The APS-associated phosphoproteins were quite similar to those associated with Grb2 and c-Cbl. The major APS binding phosphoprotein, p145 was precipitated with all other antibodies, and it is probably SHIP which is reported to be associated with Shc and Grb2 (Damen et al, 1996;Osborne et al, 1996). A marginal amount of p120 c-Cbl was precipitated with APS.…”
Section: Tyrosine Phosphorylation Of Aps and Its Associated Proteins mentioning
confidence: 92%
“…These inhibitory receptors include amongst other the CTLA-4 and CD22 expressed by T and B cells, respectively, murine FccRIIB on B and mast cells or the killer cell inhibitory receptors (KIR) on natural killer (NK) cells [1,2,3]. These receptors, upon being co-clustered with the activating receptors undergo phosphorylation of their ITIM tyrosine residues and recruit SH2 domain containing phosphatases, which interfere with the activating receptors' stimulus-response coupling cascade [1,3,4,5]. The mast cells function-associated antigen (MAFA), another inhibitory receptor has a C-type lectin domain in its extracellular part and, like the other members of the above family, its intracellular domain contains an ITIM sequence [6].…”
Section: Introductionmentioning
confidence: 99%
“…A novel role for Shc has been suggested in which phosphorylation of Y239/Y240 leads to c-myc induction and suppression of apoptosis in Ba/F3 cells, in a Ras-independent manner (Gotoh et al, 1996). The Shc PTB domain binds directly to the cytoplasmic enzyme SHIP, an SH2 domain-containing inositol 5-phosphatase, in response to growth factor and cytokine stimulation in hematopoetic cells (Damen et al, 1996;Kavanaugh et al, 1996;Lioubin et al, 1996). Furthermore, proline-rich sequences in the Shc CH1 domain are proposed to mediate the interaction between Shc and the SH3 domain of eps8, a tyrosinephosphorylated protein involved in EGF receptormediated signaling (Matoskova et al, 1995;Bon®ni et al, 1996).…”
Section: Introductionmentioning
confidence: 99%