Pez - A Novel Human cDNA Encoding Protein Tyrosine Phosphatase- and Ezrin-Like Domains

Smith, Anna; Mitchell, Phil; Shipley, Janet; Gusterson, Barry A.; Rogers, Mark V.; Crompton, M. R.

doi:10.1006/bbrc.1995.1591

Cited by 54 publications

(51 citation statements)

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“…T he protein tyrosine phosphatase Pez is the Drosophila homologue of non-receptor type protein tyrosine phosphatase 14 (PTPN14), a regulator of the TGF-b pathway [1][2][3] . PTPN14 overexpression activates TGF-b signalling and causes epithelial-mesenchymal transition (EMT) 2 .…”

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Suppressor of Deltex mediates Pez degradation and modulates Drosophila midgut homeostasis

et al. 2015

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Pez functions as an upstream negative regulator of Yorkie (Yki) to regulate intestinal stem cell (ISC) proliferation and is essential for the activity of the Hippo pathway specifically in the Drosophila midgut epithelium. Here we report that Suppressor of Deltex (Su(dx)) acts as a negative regulator of Pez. We show that Su(dx) targets Pez for degradation both in vitro and in vivo. Overexpression of Su(dx) induces proliferation in the fly midgut epithelium, which can be rescued by overexpressed Pez. We also demonstrate that the interaction between Su(dx) and Pez, bridged by WW domains and PY/PPxY motifs, is required for Su(dx)-mediated Pez degradation. Furthermore, we find that Kibra, a binding partner of Pez, stabilizes Pez via WW-PY/PPxY interaction. Moreover, PTPN14, a Pez mammalian homolog, is degraded by overexpressed Su(dx) or Su(dx) homologue WWP1 in mammalian cells. These results reveal a previously unrecognized mechanism of Pez degradation in maintaining the homeostasis of Drosophila midgut.

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Suppressor of Deltex mediates Pez degradation and modulates Drosophila midgut homeostasis

et al. 2015

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“…The PTPN14 transcript is processed into a mature mRNA in excess of 10 kb, estimated by Northern blot analysis (Smith et al, 1995). The mature transcript has a 3561 nucleotide open reading frame and ~9,2 kb 3' UTR followed by a polyadenylation site.…”

Section: Transcriptionmentioning

confidence: 99%

“…It possesses an N-terminal FERM (band 4.1, ezrin, radixin, moesin homology) domain and C-terminal catalytic domain, as well as acidic and proline-rich regions in its central uncharacterised region (Smith et al, 1995). FERM domain: the FERM domain has been shown in other proteins to be important for cytoskeletal association; however a role for the FERM domain in the PTPN14 protein has yet to be described.…”

Section: Descriptionmentioning

confidence: 99%

“…

IdentityOther names: PEZ, PTP36 HGNC (Hugo): PTPN14 Location: 1q41

DNA/RNA

DescriptionThe PTPN14 gene consists of 19 exons and 21 introns divided over 203 kb, including a coding region and 5' and 3' non-coding regions.

TranscriptionThe PTPN14 transcript is processed into a mature mRNA in excess of 10 kb, estimated by Northern blot analysis (Smith et al, 1995). The mature transcript has a 3561 nucleotide open reading frame and ~9,2 kb 3' UTR followed by a polyadenylation site.

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PTPN14 (protein tyrosine phosphatase, non-receptor type 14)

Hauschild¹,

Belle²,

Khew‐Goodall³

2013

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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IdentityOther names: PEZ, PTP36 HGNC (Hugo): PTPN14 Location: 1q41 DNA/RNA DescriptionThe PTPN14 gene consists of 19 exons and 21 introns divided over 203 kb, including a coding region and 5' and 3' non-coding regions. TranscriptionThe PTPN14 transcript is processed into a mature mRNA in excess of 10 kb, estimated by Northern blot analysis (Smith et al., 1995). The mature transcript has a 3561 nucleotide open reading frame and ~9,2 kb 3' UTR followed by a polyadenylation site. No transcript variants have been identified. Little investigation has been undertaken to elucidate the factors regulating PTPN14 transcription. However, real-time PCR and ChIP sequencing have shown that p63 induces PTPN14 expression by binding to a p63 consensus sequence within intron 3 of PTPN14 (Perez et al., 2007).Genomic and transcript structure of human PTPN14. A. The genomic arrangement of PTPN14 with vertical bars depicting the location and relative size of exons. Space between exons depicts relative sizes of introns/non-coding regions. B. The mature transcript arrangement of PTPN14. Exons are numbered and coding regions are depicted in light brown, with non-coding regions depicted in red.

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“…Pez is a non-receptor protein tyrosine phosphatase (PTP), 1 which has until recently remained fairly poorly characterised in terms of elucidation of a defined cellular function. Pez (also known as PTPD2 2 and PTPN14, 3 in human and PTP36 in the mouse 4 has been found to localise to multiple sub-cellular locations, depending on factors such as cell type, cell-matrix adhesion, 4 serine phosphorylation 5 and cell confluency, 6 suggesting differential regulation of Pez function in alternative cell states and cellular contexts.…”

Section: Introductionmentioning

confidence: 99%

PTP-Pez: A novel regulator of TGFβ signaling

Wyatt¹,

Khew‐Goodall²

2008

Cell Cycle

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The TGFβs are a family of pleiotropic cytokines that mediate diverse effects including the regulation of cell cycle progression, apoptosis, tissue remodelling and epithelial-mesenchymal transition (EMT). These diverse effects allow the TGFβs to play multiple and even opposing roles in different contexts during embryonal development, tissue homeostasis and cancer progression. We recently reported that the protein tyrosine phosphatase Pez is a novel inducer of TGFβ signaling, regulating EMT and organogenesis in developing zebrafish embryos, and leading to TGFβ-mediated EMT when overexpressed in vitro in epithelial MDCK cells. A number of mutations in Pez have been shown to be associated with breast and colorectal cancers, although the effect of these mutations on Pez function and their contribution to cancer progression remains unclear. Our finding that Pez regulates TGFβ signaling is therefore of interest not only in the context of identifying a novel upstream regulator of TGFβ signaling, but also in implicating the dysregulation of TGFβ signaling as a possible link between Pez mutation and cancer progression. Here we discuss the implications of our research, in the context of dysregulation of TGFβ signaling in cancer and other human pathologies.

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Pez - A Novel Human cDNA Encoding Protein Tyrosine Phosphatase- and Ezrin-Like Domains

Cited by 54 publications

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Suppressor of Deltex mediates Pez degradation and modulates Drosophila midgut homeostasis

Suppressor of Deltex mediates Pez degradation and modulates Drosophila midgut homeostasis

PTPN14 (protein tyrosine phosphatase, non-receptor type 14)

PTP-Pez: A novel regulator of TGFβ signaling

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Pez - A Novel Human cDNA Encoding Protein Tyrosine Phosphatase- and Ezrin-Like Domains

Cited by 54 publications

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Suppressor of Deltex mediates Pez degradation and modulates Drosophila midgut homeostasis

Suppressor of Deltex mediates Pez degradation and modulates Drosophila midgut homeostasis

PTPN14 (protein tyrosine phosphatase, non-receptor type 14)

PTP-Pez: A novel regulator of TGF&beta; signaling

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PTP-Pez: A novel regulator of TGFβ signaling