Tensin2 reduces intracellular phosphatidylinositol 3,4,5-trisphosphate levels at the plasma membrane

Hafizi, Sassan; Gustafsson, Anna; Oslakovic, Cecilia; Idevall‐Hagren, Olof; Tengholm, Anders; Spérandio, Olivier; Villoutreix, Bruno O.; Dahlbäck, Björn

doi:10.1016/j.bbrc.2010.07.085

Cited by 15 publications

(24 citation statements)

References 17 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Some studies suggest that C1-Ten is a positive regulator of cell migration (49) and proliferation by Akt activation (50), but other studies suggest that C1-Ten is a negative regulator of cell migration and proliferation through inhibition of Akt (24). On the basis of our findings, the true effect of C1-Ten on Akt activation may depend on the contribution of IRS-1 and the basal state of cells, such as whether the IGF autocrine pathway is activated.…”

Section: Discussionmentioning

confidence: 50%

See 1 more Smart Citation

C1-Ten Is a Protein Tyrosine Phosphatase of Insulin Receptor Substrate 1 (IRS-1), Regulating IRS-1 Stability and Muscle Atrophy

Koh

Lee

Yang

et al. 2013

Molecular and Cellular Biology

View full text Add to dashboard Cite

f Muscle atrophy occurs under various catabolic conditions, including insulin deficiency, insulin resistance, or increased levels of glucocorticoids. This results from reduced levels of insulin receptor substrate 1 (IRS-1), leading to decreased phosphatidylinositol 3-kinase activity and thereby activation of FoxO transcription factors. However, the precise mechanism of reduced IRS-1 under a catabolic condition is unknown. Here, we report that C1-Ten is a novel protein tyrosine phosphatase (PTPase) of IRS-1 that acts as a mediator to reduce IRS-1 under a catabolic condition, resulting in muscle atrophy. C1-Ten preferentially dephosphorylated Y612 of IRS-1, which accelerated IRS-1 degradation. These findings suggest a novel type of IRS-1 degradation mechanism which is dependent on C1-Ten and extends our understanding of the molecular mechanism of muscle atrophy under catabolic conditions. C1-Ten expression is increased by catabolic glucocorticoid and decreased by anabolic insulin. Reflecting these hormonal regulations, the muscle C1-Ten is upregulated in atrophy but downregulated in hypertrophy. This reveals a previously unidentified role of C1-Ten as a relevant PTPase contributing to skeletal muscle atrophy.

show abstract

Section: Discussionmentioning

confidence: 50%

“…In addition, C1-Ten possesses a C1 domain. Recent papers suggested that only C1-Ten, but not tensin3, has a PTEN-like activity in the cells (23,24). However, there is no evidence that C1-Ten is a direct lipid phosphatase like PTEN is.…”

mentioning

confidence: 99%

C1-Ten Is a Protein Tyrosine Phosphatase of Insulin Receptor Substrate 1 (IRS-1), Regulating IRS-1 Stability and Muscle Atrophy

Koh

Lee

Yang

et al. 2013

Molecular and Cellular Biology

View full text Add to dashboard Cite

show abstract

“…Tenc1 is a cytoplasmic phosphoprotein that is localized to integrin-mediated focal adhesions [19,20]. Tenc1 contains PTB and SH2 domains at the C terminus that interact with tyrosine-phosphorylated proteins, PKC and actin-binding domains at the N terminus, but the center region of Tenc1 does not contain the actin-capping domain present in tensin1, suggesting that it is not able to regulate actin polymerization [19,20,21,22]. In addition, Tenc1 has a phosphatase and a C2 domain pairing, which is homologous to phosphatase and the tensin homolog [19,20,21,22].…”

Section: Discussionmentioning

confidence: 99%

“…Tenc1, a member of the tensin family, is an integrin-mediated focal adhesion molecule that regulates cell migration [19,20]. Tenc1 possesses a protein kinase C (PKC)- and actin-binding domain at the N terminus, src homology 2 (SH2), and phosphotyrosine-binding (PTB) domains at the C terminus, and is widely distributed in mouse tissues including the heart, liver, kidney and skeletal muscle [19,20,21,22]. The function of Tenc1 in the kidney and its involvement in the development of nephrotic syndrome remain poorly understood [23,24].…”

Section: Introductionmentioning

confidence: 99%

Tenc1-Deficient Mice Develop Glomerular Disease in a Strain-Specific Manner

Uchio‐Yamada

Sawada

Tamura

et al. 2013

Nephron Exp Nephrol

View full text Add to dashboard Cite

Background/Aims: Tenc1 (also known as tensin2) is an integrin-associated focal adhesion molecule that is broadly expressed in mouse tissues including the liver, muscle, heart and kidney. A mouse strain carrying mutated Tenc1, the ICR-derived glomerulonephritis (ICGN) strain, develops severe nephrotic syndrome. Methods: To elucidate the function of Tenc1 in the kidney, Tenc1^ICGN was introduced into 2 genetic backgrounds, i.e. DBA/2J (D2) and C57BL/6J (B6), strains that are respectively susceptible and resistant to chronic kidney disease. Results: Biochemical and histological analysis revealed that homozygous Tenc1^ICGN mice develop nephrotic syndrome on the D2 background (D2GN) but not on the B6 background (B6GN). Initially, abnormal assembly and maturation of glomerular basement membrane (GBM) were observed, and subsequently effacement of podocyte foot processes was noted in the kidneys of D2GN but not B6GN mice. These defects are likely to be involved in the integrin signaling pathway. Conclusion: This study suggests that Tenc1 contributes to the maintenance of GBM structures and that the genetic background influences the severity of nephrotic syndrome.

show abstract

“…GSK3 ␤ inhibits SREBF activity by phosphorylation, triggering targeted ubiquitination and proteosomal degradation ( 42 ). In contrast, TENC1 phosphotase, upregulated in low LDL-C baboon responders, dephosphorylates PIP3 to PIP2, inhibiting AKT1 activation ( 43 ). Consequently, the ability of GSK3 ␤ to inhibit SREBF transcription activity is enhanced, and the result is reduced blot and observed that TENC1 expression is in concordance with mRNA levels.…”

Section: Quantifi Cation Of Protein Expressionmentioning

confidence: 91%