Cellular phosphatase activity of C1-Ten/Tensin2 is controlled by Phosphatidylinositol-3,4,5-triphosphate binding through the C1-Ten/Tensin2 SH2 domain

Kim, Eui; Kim, Do Hyeon; Singaram, Indira; Jeong, Heeyoon; Koh, Ara; Lee, Jiyoun; Cho, Wonhwa; Ryu, Sung Ho

doi:10.1016/j.cellsig.2018.07.009

Cited by 12 publications

(13 citation statements)

References 55 publications

(73 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Tensin‐2 retains the cysteine residue, but lost the histidine and arginine residues. There is evidence that tensin‐2 might be catalytically active, as it was shown to bind to PI(3,4,5)P 3 , which was shown to increase its ability to dephosphorylate IRS1 and to regulate insulin receptor signaling [144,145]. Thus, tensin‐2 is potentially a catalytically active pseudophosphatase.…”

Section: Pseudoenzymes Within the Cc1‐fold Phosphatase Familymentioning

confidence: 99%

The dead phosphatases society: a review of the emerging roles of pseudophosphatases

et al. 2020

View full text Add to dashboard Cite

Phosphatases are a diverse family of enzymes, comprising at least 10 distinct protein folds. Like most other enzyme families, many have sequence variations that predict an impairment or loss of catalytic activity classifying them as pseudophosphatases. Research on pseudoenzymes is an emerging area of interest, with new biological functions repurposed from catalytically active relatives. Here, we provide an overview of the pseudophosphatases identified to date in all major phosphatase families. We will highlight the degeneration of the various catalytic sequence motifs and discuss the challenges associated with the experimental determination of catalytic inactivity. We will also summarize the role of pseudophosphatases in various diseases and discuss the major challenges and future directions in this field.

show abstract

Section: Pseudoenzymes Within the Cc1‐fold Phosphatase Familymentioning

confidence: 99%

The dead phosphatases society: a review of the emerging roles of pseudophosphatases

et al. 2020

View full text Add to dashboard Cite

show abstract

“…Based on the results of their previous systematic study on SH2 domain lipid binding, Kim et al have investigated C1-Ten/Tensin2 [ 53 ]. This protein is highly similar in amino acid sequence and domain organization to Tensin [ 54 ].…”

Section: Many Sh2 Domains Themselves Browse Membrane Lipids Besides Tyrosine Phosphorylated Proteins To Find the Matching Partnersmentioning

confidence: 99%

“…It preferentially dephosphorylates Y612 of IRS-1, which is associated with accelerated IRS-1 degradation. In their study, Kim et al found that C1-Ten/Tensin2 attenuates IRS-1 phosphorylation in a PI3K-dependent manner [ 53 ]. Structural analyses of the C1-Ten/Tensin2 SH2 domain have suggested that it also possesses a distinct cationic patch formed by K1147, K1155, and K1157, which is far from the pY-binding pocket.…”

Section: Many Sh2 Domains Themselves Browse Membrane Lipids Besides Tyrosine Phosphorylated Proteins To Find the Matching Partnersmentioning

confidence: 99%

“…These results suggest that phosphatidylinositol-3,4,5-trisphosphate engagement via the SH2 domain is important for sustained ZAP70 activity but not for activation itself [45]. Based on the results of their previous systematic study on SH2 domain lipid binding, Kim et al have investigated C1-Ten/Tensin2 [53]. This protein is highly similar in amino acid sequence and domain organization to Tensin [54].…”

Section: Figurementioning

confidence: 99%

See 1 more Smart Citation

Novel Roles of SH2 and SH3 Domains in Lipid Binding

Sipeki

Koprivanacz

Takács

et al. 2021

Cells

View full text Add to dashboard Cite

Signal transduction, the ability of cells to perceive information from the surroundings and alter behavior in response, is an essential property of life. Studies on tyrosine kinase action fundamentally changed our concept of cellular regulation. The induced assembly of subcellular hubs via the recognition of local protein or lipid modifications by modular protein interactions is now a central paradigm in signaling. Such molecular interactions are mediated by specific protein interaction domains. The first such domain identified was the SH2 domain, which was postulated to be a reader capable of finding and binding protein partners displaying phosphorylated tyrosine side chains. The SH3 domain was found to be involved in the formation of stable protein sub-complexes by constitutively attaching to proline-rich surfaces on its binding partners. The SH2 and SH3 domains have thus served as the prototypes for a diverse collection of interaction domains that recognize not only proteins but also lipids, nucleic acids, and small molecules. It has also been found that particular SH2 and SH3 domains themselves might also bind to and rely on lipids to modulate complex assembly. Some lipid-binding properties of SH2 and SH3 domains are reviewed here.

show abstract

“…has also been reported to influence the phosphorylation of IRS-1 (insulin receptor substrate 1) via binding to phosphatidylinositol-3,4,5-triphosphate, therefore contributing to the regulation of insulin signalling pathways (Kim et al, 2018). (Hong et al, 2016).…”

Section: Tensinmentioning

confidence: 99%

Untitled

Supplemental Information 5: Figure 5 - TNS3 and TNS4 Upregulation

View full text Add to dashboard Cite

Tensins are structural adaptor proteins localized at focal adhesions. Tensins can act as mechanosensors and participate in the transduction of biochemical signals from the extracellular matrix to the cytoskeleton, acting as an interface able to alter cell behavior in responses to changes in their surrounding environment. This review aims to provide a concise summary of the main functions of the four known tensins in cell and cancer biology, their homology and recently unveiled signaling mechanisms. We focus specifically on how tensin 4 (TNS4/Cten) may contribute to cancer both as an oncogene supporting metastasis and as tumour suppressor in different types of tissue. A better understanding of the cancer mechanistics involving tensins may provide the rationale for development of specific therapeutic strategies.

show abstract

Cellular phosphatase activity of C1-Ten/Tensin2 is controlled by Phosphatidylinositol-3,4,5-triphosphate binding through the C1-Ten/Tensin2 SH2 domain

Cited by 12 publications

References 55 publications

The dead phosphatases society: a review of the emerging roles of pseudophosphatases

The dead phosphatases society: a review of the emerging roles of pseudophosphatases

Novel Roles of SH2 and SH3 Domains in Lipid Binding

Untitled

Contact Info

Product

Resources

About