The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence

Frangioni, John V.; Beahm, Pamela H.; Shifrin, Victor; Jost, Christine A.; Neel, Benjamin G.

doi:10.1016/0092-8674(92)90190-n

Cited by 560 publications

(482 citation statements)

References 38 publications

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“…Tyrosine 66 is the major target for phosphorylation of PTP1B by the insulin receptor, creating a site essential for downstream signaling (Bandyopadhyay et al, 1997). The carboxy terminus of PTP1B directs its localization to the cytosolic face of the endoplasmic reticulum (Frangioni et al, 1992). In platelets and activated T cells, proteolytic cleavage in the ER targeting domain results in translocation of PTP1B to the cytoskeletal/membrane fraction (Frangioni et al, 1993;Ezumi et al, 1995;Rock et al, 1997).…”

Section: Maintaining Stable Adhesions: the Nonreceptor Tyrosine Kinasmentioning

confidence: 99%

Turn‐off, drop‐out: Functional state switching of cadherins

Lilien

Balsamo

Arregui

et al. 2002

Developmental Dynamics

149

116

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The classic cadherins are a group of calcium dependent, homophilic cell-cell adhesion molecules that drive morphogenetic rearrangements and maintain the integrity of cell groups through the formation of adherens junctions. The formation and maintenance of cadherin-mediated adhesions is a multistep process and mechanisms have evolved to regulate each step. This suggests that functional state switching plays an important role in development. Among the many challenges ahead is to determine the developmental role that functional state switching plays in tissue morphogenesis and to define the roles of each of the several regulatory interactions that participate in switching. One correlate of the loss of cadherinmediated adhesion, the "turn-off" of cadherin function, is the exit, or "drop-out" of cells from neural and epithelial layers and their conversion to a motile phenotype. We suggest that epithelial mesenchymal conversions may be initiated by signaling pathways that result in the loss of cadherin function. Tyrosine phosphorylation of ␤-catenin is one such mechanism. Enhanced phosphorylation of tyrosine residues on ␤-catenin is almost invariably associated with loss of the cadherin-actin connection concomitant with loss of adhesive function. There are several tyrosine kinases and phosphatases that have been shown to have the potential to alter the phosphorylation state of ␤-catenin and thus the function of cadherins. Our laboratory has focused on the role of the nonreceptor tyrosine phosphatase PTP1B in regulating the phosphorylation of ␤-catenin on tyrosine residues. Our data suggest that PTP1B is crucial for maintenance of N-cadherin-mediated adhesions in embryonic neural retina cells. By using an L-cell model system constitutively expressing N-cadherin, we have worked out many of the molecular interactions essential for this regulatory interaction. Extracellular cues that bias this critical regulatory interaction toward increased phosphorylation of ␤-catenin may be a critical component of many developmental events.

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Section: Maintaining Stable Adhesions: the Nonreceptor Tyrosine Kinasmentioning

confidence: 99%

Turn‐off, drop‐out: Functional state switching of cadherins

Lilien

Balsamo

Arregui

et al. 2002

Developmental Dynamics

149

116

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“…One important example is that of PTP1B, which was initially described as a 37 kDa protein with tyrosine speci®c protein phosphatase activity (Tonks et al, 1988). Subsequent studies demonstrate that this puri®ed protein represented a truncated form of a 50 kDa enzyme which was later shown to be associated with the endoplasmic reticulum (ER) (and other membranous organelles) through hydrophobic interaction of its C-terminus with the cytoplasmic face of the ER membrane (Frangioni et al, 1992). Studies have shown that PTP1B is a cellular substrate of several protein kinases involved in cell cycle regulation, stress responses and signal transduction including recent reports of its tyrosine phosphorylation by insulin and other growth factors which may regulate PTP1B enzymatic activity (Flint et al, 1993;Shifrin et al, 1997;Bandyopadhyay et al, 1997;Liu and Cherno , 1997).…”

Section: Introductionmentioning

confidence: 99%

“…Studies have shown that PTP1B is a cellular substrate of several protein kinases involved in cell cycle regulation, stress responses and signal transduction including recent reports of its tyrosine phosphorylation by insulin and other growth factors which may regulate PTP1B enzymatic activity (Flint et al, 1993;Shifrin et al, 1997;Bandyopadhyay et al, 1997;Liu and Cherno , 1997). Other studies have shown that limited and speci®c proteolysis of PTP1B stimulates its enzymatic activity, possibly through disruption of its membrane association (Frangioni et al, 1992(Frangioni et al, , 1993. Studies have shown that the extent or site of proteolysis of PTP1B may control its access to distinct cellular substrates.…”

Section: Introductionmentioning

confidence: 99%

Differential expression and translocation of protein tyrosine phosphatase 1B-related proteins in ME-180 tumor cells expressing apoptotic sensitivity and resistance to tumor necrosis factor: potential interaction with epidermal growth factor receptor

1999

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“…1 Protein tyrosine phosphatase 1B is a key regulator of metabolism and cell growth by its ability to dephosphorylate receptors of the tyrosine kinase superfamily and modulate the duration and intensity of the signals emerging from these activated receptors. As demonstrated by genetic and biochemical approaches, PTP1B dephosphorylates and inactivates the epidermal growth factor receptor (EGFR), 2 the platelet-derived growth factor receptor, 3 the hepatocyte growth factor receptor (HGFR), 4 the insulin receptor (IR), 5 and the insulin-like growth factor-1 receptor.…”

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confidence: 99%

Protein Tyrosine Phosphatase 1B (PTP1B) Deficiency Accelerates Hepatic Regeneration in Mice

Revuelta-Cervantes

Mayoral

Miranda

et al. 2011

The American Journal of Pathology

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Protein tyrosine phosphatase 1B (PTP1B) is a key regulator of metabolism and cell growth by its ability to dephosphorylate tyrosine kinase receptors and modulate the intensity of their signaling cascades. Because liver regeneration involves tyrosine phosphorylation-mediated signaling, we investigated the role of PTP1B in this process by performing partial hepatectomy in wild-type (PTP1B ؉/؉ ) and PTP1B-deficient (PTP1B ؊/؊ ) mice. The expression of PCNA and cyclins D1 and E (cell proliferation markers) was enhanced in PTP1B ؊/؊ regenerating livers, in parallel with 5=-bromo-2=-deoxyuridine incorporation. Phosphorylation of JNK1/2 and STAT3, early triggers of hepatic regeneration in response to TNF-␣ and IL-6, was accelerated in PTP1B ؊/؊ mice compared with PTP1B ؉/؉ mice. These phosphorylations were increased in PTP1B ؊/؊ hepatocytes or by silencing PTP1B in wild-type cells and decreased further after the addition of recombinant PTP1B. Enhanced EGFand HGF receptor-mediated signaling was observed in regenerating livers lacking PTP1B and in EGF-or HGF-stimulated PTP1B ؊/؊ hepatocytes. Moreover, PTP1B ؊/؊ mice displayed a more rapid increase in intrahepatic lipid accumulation than PTP1B ؉/؉ control mice. Late responses to partial hepatectomy revealed additional divergences because stress-mediated signaling was attenuated at 24 to 96 hours in PTP1B ؊/؊ mice compared with PTP1B ؉/؉ mice. Finally, PTP1B deficiency also improves hepatic regeneration in mice fed a high-fat diet. These results suggest that pharmacological inhibition of PTP1B would improve liver regeneration in patients with acute or chronic liver injury.

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The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence

Cited by 560 publications

References 38 publications

Turn‐off, drop‐out: Functional state switching of cadherins

Turn‐off, drop‐out: Functional state switching of cadherins

Differential expression and translocation of protein tyrosine phosphatase 1B-related proteins in ME-180 tumor cells expressing apoptotic sensitivity and resistance to tumor necrosis factor: potential interaction with epidermal growth factor receptor

Protein Tyrosine Phosphatase 1B (PTP1B) Deficiency Accelerates Hepatic Regeneration in Mice

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