A c-Cbl Yeast Two Hybrid Screen Reveals Interactions with 14-3-3 Isoforms and Cytoskeletal Components

Robertson, H. M.; Langdon, Wallace Y.; Thien, Christine B.F.; Bowtell, David D.L.

doi:10.1006/bbrc.1997.7608

Cited by 25 publications

(11 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Finally, these results further suggest that ITSN may be linked to the ubiquitination pathway. This notion is supported by the ®nding that Cbl, an E3-ubiquitin ligase involved in RTK regulation (see review this issue), interacts with the SH3 domains of ITSN by yeast two-hybrid analysis (Robertson et al, 1997) as well by co-immunoprecipitation and in vitro binding analysis (RP Mohney, manuscript in preparation).…”

Section: Itsn Stimulates Mitogenic Signaling Pathwaysmentioning

confidence: 91%

Mitogenesis and endocytosis: What's at the INTERSECTIoN?

2001

View full text Add to dashboard Cite

Section: Itsn Stimulates Mitogenic Signaling Pathwaysmentioning

confidence: 91%

Mitogenesis and endocytosis: What's at the INTERSECTIoN?

2001

View full text Add to dashboard Cite

“…Furthermore, a yeast two hybrid screen (Robertson et al, 1997) uncovered interactions between c-Cbl and two proteins involved in receptor endocytosis: unconventional myosin 1C (Bement et al, 1994), required for endocytosis of the afactor receptor in yeast (Geli and Riezman, 1996); and Ese1, a homologue of Drosophila Dap160, which interacts with dynamin through one of its four SH3 domains (Roos and Kelly, 1998) and functions in receptor endocytosis in both yeast and mammals (Sengar et al, 1999;Wendland and Emr, 1998). The interaction between Dv-cbl and Dap160, was tested genetically using EP element insertions in the Dap160 locus.…”

Section: A Screen Reveals Interactions Between D-cbl and Other Negatimentioning

confidence: 99%

A Drosophila analogue of v-Cbl is a dominant-negative oncoprotein in vivo

et al. 2000

Self Cite

View full text Add to dashboard Cite

“…One such example is c-Cbl. Other proteins that have been reported to be associated in a complex with c-Cbl include Bruton's tyrosine kinase (61), c-Cbl-associated protein (60), Vav (62), SHIP (63), SHP-2 (64), JAK2, 3 Syk protein tyrosine kinase (58), ZAP-70 tyrosine kinase (59), Crk-L (65), Sam68, JAK3, and phospholipase C ␥1 (66), Tyk-2 (67), 14-3-3 protein isoforms, cytokeratin 18, human unconventional myosin IC, and SH3 P17 (68). Whether GH utilizes all of these signaling molecules as well, in what cell type, and in what combination remains to be determined.…”

mentioning

confidence: 99%

Growth Hormone Stimulates the Formation of a Multiprotein Signaling Complex Involving p130Cas and CrkII

Zhu¹,

Goh²,

LeRoith³

et al. 1998

Journal of Biological Chemistry

View full text Add to dashboard Cite

We have demonstrated previously that growth hormone (GH) activates focal adhesion kinase (FAK), and this activation results in the tyrosine phosphorylation of two FAK substrates, namely paxillin and tensin. We now show here in Chinese hamster ovary cells stably transfected with rat GH receptor cDNA that human (h)GH induces the formation of a large multiprotein signaling complex centered around another FAK-associated protein, p130Cas and the adaptor protein CrkII. hGH stimulates the tyrosine phosphorylation of both p130Cas and CrkII, their association, and the association of multiple other tyrosine-phosphorylated proteins to the complex. Growth hormone (GH)1 is the major regulator of postnatal body growth (1). It possesses diverse and pleiotropic effects on the growth, differentiation, and metabolism of cells. GH is thought to initiate its biological actions, including induction of a number of RNA species in mammalian tissues by interaction with a specific membrane-bound receptor (2). The GH receptor is phosphorylated upon ligand stimulation presumably by the physical association of the nonreceptor tyrosine kinase JAK2 (3). The JAK kinases are linked to transcriptional regulation and JAK activation results in the phosphorylation, dimerization, and nuclear translocation of latent cytoplasmic STAT transcription factors (4). The activated STAT factors bind to their appropriate DNA-responsive elements to activate gene transcription (4). Other diverse actions of GH include the stimulation of chemotaxis and migration of monocytic cells (5). Concordantly, we have demonstrated that GH stimulates the re-organization of the actin cytoskeleton in cells with fibroblastic morphology (6) and reported that this re-organization of the actin cytoskeleton requires the activity of PI 3-kinase.Focal adhesion kinase (p125 FAK ) has been postulated to play a central role in the response of the cell to the extracellular matrix (for review, see Ref. 7) and in cell morphology and motility (for review, see Ref. 8). For example, overexpression of FAK stimulates cell migration (9) and both FAK-deficient endodermal and mesodermal cells migrate slower than their FAK replete counterparts (10, 11). The effect of FAK on the cytoskeleton is presumably mediated by the formation of a p130Cas (Crk-associated substrate)-CrkII complex (12) in association with c-Src (for review, see Ref. 13). We have reported recently that GH stimulates the tyrosine phosphorylation of FAK and two of its substrates, paxillin and tensin, and that FAK associates with JAK2 and requires the JAK2 binding site on the GH receptor for its phosphorylation (14). We demonstrate here that hGH also stimulates the tyrosine phosphorylation of both p130Cas and CrkII, their association, and the association of multiple other tyrosine-phosphorylated proteins to the complex including the c-Src and c-Fyn protein-tyrosine kinases, Nck, c-Cbl, tensin, paxillin, IRS-1, the p85 subunit of PI 3-kinase, SHC, Grb-2, Sos-1, and C3G. Finally we demonstrate that JNK/SAPK is activated in response to ...

show abstract

A c-Cbl Yeast Two Hybrid Screen Reveals Interactions with 14-3-3 Isoforms and Cytoskeletal Components

Cited by 25 publications

References 34 publications

Mitogenesis and endocytosis: What's at the INTERSECTIoN?

Mitogenesis and endocytosis: What's at the INTERSECTIoN?

A Drosophila analogue of v-Cbl is a dominant-negative oncoprotein in vivo

Growth Hormone Stimulates the Formation of a Multiprotein Signaling Complex Involving p130Cas and CrkII

Contact Info

Product

Resources

About