Interaction of 14-3-3 proteins with the insulin-like growth factor I receptor (IGFIR): evidence for a role of 14-3-3 proteins in IGFIR signaling

Spence, Susan L.; Dey, Bhakta R.; Terry, Cheryl; Albert, Paul S.; Nissley, Peter; Furlanetto, Richard W.

doi:10.1016/j.bbrc.2003.11.043

Cited by 14 publications

(9 citation statements)

References 20 publications

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“…A separate study reported that the major difference between IGFR and IR was in their potential to recruit SHP2 (Hanke and Mann, 2009). It has also been reported that 14-3-3 interacts specifically with IGFR, via S1283, but not with IR (Furlanetto et al, 1997), and this may contribute to anti-apoptotic signaling (Peruzzi et al, 1999) and transformation pathways (Spence et al, 2003). A PDZ protein IIP-1/GIPC, identified as a binding partner for the C-terminal tail of IGFR but not IR (Ligensa et al, 2001), was suggested to couple IGFR to G i (Booth et al, 2002) and more recently was implicated in ROS generation (Choi et al, 2010).…”

Section: Non-substrate Receptor Associations: Adaptors and Scaffoldsmentioning

confidence: 98%

“…Serine phosphorylation of IR may contribute to development of insulin resistance, for instance as a consequence of hyperglycemia (Kellerer and Haring, 1995). Serine phosphorylation of IGFR may result in 14-3-3 binding, affecting both signaling and receptor turnover (Furlanetto et al, 1997; Spence et al, 2003). However, the sites, mechanisms, and consequences of IR/IGFR serine/threonine phosphorylation have never been well defined and there have been few recent studies in this area.…”

Section: Negative and Feedback Regulationmentioning

confidence: 99%

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Molecular Basis of Signaling Specificity of Insulin and IGF Receptors: Neglected Corners and Recent Advances

2012

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Insulin and insulin-like growth factor (IGF) receptors utilize common phosphoinositide 3-kinase/Akt and Ras/extracellular signal-regulated kinase signaling pathways to mediate a broad spectrum of “metabolic” and “mitogenic” responses. Specificity of insulin and IGF action in vivo must in part reflect expression of receptors and responsive pathways in different tissues but it is widely assumed that it is also determined by the ligand binding and signaling mechanisms of the receptors. This review focuses on receptor-proximal events in insulin/IGF signaling and examines their contribution to specificity of downstream responses. Insulin and IGF receptors may differ subtly in the efficiency with which they recruit their major substrates (IRS-1 and IRS-2 and Shc) and this could influence effectiveness of signaling to “metabolic” and “mitogenic” responses. Other substrates (Grb2-associated binder, downstream of kinases, SH2Bs, Crk), scaffolds (RACK1, β-arrestins, cytohesins), and pathways (non-receptor tyrosine kinases, phosphoinositide kinases, reactive oxygen species) have been less widely studied. Some of these components appear to be specifically involved in “metabolic” or “mitogenic” signaling but it has not been shown that this reflects receptor-preferential interaction. Very few receptor-specific interactions have been characterized, and their roles in signaling are unclear. Signaling specificity might also be imparted by differences in intracellular trafficking or feedback regulation of receptors, but few studies have directly addressed this possibility. Although published data are not wholly conclusive, no evidence has yet emerged for signaling mechanisms that are specifically engaged by insulin receptors but not IGF receptors or vice versa, and there is only limited evidence for differential activation of signaling mechanisms that are common to both receptors. Cellular context, rather than intrinsic receptor activity, therefore appears to be the major determinant of whether responses to insulin and IGFs are perceived as “metabolic” or “mitogenic.”

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Section: Non-substrate Receptor Associations: Adaptors and Scaffoldsmentioning

confidence: 98%

Section: Negative and Feedback Regulationmentioning

confidence: 99%

Molecular Basis of Signaling Specificity of Insulin and IGF Receptors: Neglected Corners and Recent Advances

2012

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“…The major site for 14-3-3ζ and β interaction with IGF1R occurs within a serine rich region that is critical for IGF1R mediated cell transformation 52. Mutation of the 14-3-3 binding site in IGF1R blocked colony formation in a soft agar assay and reduced the tumorigenicity in mice, suggesting 14-3-3ζ and/or β may contribute to IGF1R mediated transformation 53. The tuberous sclerosis (TSC) protein 1 and 2 are involved in tumor suppression by inhibiting ribosomal subunit S6 kinase (S6K) signaling pathways.…”

Section: 14-3-3 Targets In Cancermentioning

confidence: 99%

14-3-3ζ as a prognostic marker and therapeutic target for cancer

Neal

2010

Expert Opinion on Therapeutic Targets

112

114

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Importance of the field The ubiquitously expressed 14-3-3ζ protein is involved in numerous important cellular pathways involved in cancer. Recent research suggests 14-3-3ζ may play a central role regulating multiple pathways responsible for cancer initiation and progression. This review will provide an overview of 14-3-3 proteins and address the role of 14-3-3ζ overexpression in cancer. Areas covered in this review The review covers the basic role of 14-3-3 in regulation of multiple pathways with a focus on 14-3-3ζ as a clinically relevant biomarker for cancer recurrence. What the reader will gain 14-3-3ζ overexpression has been found in multiple cancers; however, the clinical implications were unclear. Recently, 14-3-3ζ has been identified as a biomarker for poor prognosis and chemoresistance in multiple tumor types, indicating a potential clinical application for using 14-3-3ζ in selecting treatment options and predicting cancer patients’ outcome. Take home message 14-3-3ζ is a potential prognostic marker of cancer recurrence and predictive marker for therapeutic resistance. The overexpression of 14-3-3ζ in multiple cancers suggests that it may be a common target to intervene tumor progression; therefore, more efforts are needed for the development of 14-3-3 inhibitors.

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“…Transfection of the cells with antisense 14-3-3␤ cDNA diminished their growth ability in vitro as well as in vivo after inoculation in nude mice [38]. Interestingly, 14-3-3␤ interacts with the insulin-like growth factor I receptor (IGFIR) and thus may play an important role in the transformation pathway signaled by IGFIR [39]. This leads to the assumption that in the malignant thyroid cell IGFIR-whose expression has been demonstrated especially in thyroid tumors with aggressive clinical behavior [40]-may also be regulated by 14-3-3␤ protein.…”

Section: -3-3␤/ywhabmentioning

confidence: 97%

Identification of Differentially Expressed Genes in Papillary Thyroid Carcinomas With and Without Rearrangements of the Tyrosine Kinase Receptors RET and/or NTRK1

Musholt

Brehm

Hanack

et al. 2006

Journal of Surgical Research

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Interaction of 14-3-3 proteins with the insulin-like growth factor I receptor (IGFIR): evidence for a role of 14-3-3 proteins in IGFIR signaling

Cited by 14 publications

References 20 publications

Molecular Basis of Signaling Specificity of Insulin and IGF Receptors: Neglected Corners and Recent Advances

Molecular Basis of Signaling Specificity of Insulin and IGF Receptors: Neglected Corners and Recent Advances

14-3-3ζ as a prognostic marker and therapeutic target for cancer

Identification of Differentially Expressed Genes in Papillary Thyroid Carcinomas With and Without Rearrangements of the Tyrosine Kinase Receptors RET and/or NTRK1

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