FNTA{farnesyltransferase, CAAX box, alpha}rabbit.pAb
- Known as:
- FNTA{farnesyltransferase, CAAX box, a}host: rabbit.pAb
- Catalog number:
- 201-20-2092
- Product Quantity:
- 0.2ml
- Category:
- -
- Supplier:
- Shanghai Sunred
- Gene target:
- FNTA{farnesyltransferase CAAX box alpha}rabbit.pAb
Related genes to: FNTA{farnesyltransferase, CAAX box, alpha}rabbit.pAb
- Gene:
- PTP4A1 NIH gene
- Name:
- protein tyrosine phosphatase 4A1
- Previous symbol:
- -
- Synonyms:
- PTPCAAX1, PRL-1, PRL1
- Chromosome:
- 6q12
- Locus Type:
- gene with protein product
- Date approved:
- 1998-09-02
- Date modifiied:
- 2019-02-14
- Gene:
- PTP4A2 NIH gene
- Name:
- protein tyrosine phosphatase 4A2
- Previous symbol:
- PTP4A
- Synonyms:
- HU-PP-1, PTPCAAX2, OV-1, ptp-IV1a, PRL-2, PRL2
- Chromosome:
- 1p35.2
- Locus Type:
- gene with protein product
- Date approved:
- 1996-03-14
- Date modifiied:
- 2019-02-14
Related products to: FNTA{farnesyltransferase, CAAX box, alpha}rabbit.pAb
Related articles to: FNTA{farnesyltransferase, CAAX box, alpha}rabbit.pAb
- The phosphatase and tensin homolog deleted on chromosome 10 (PTEN) is one of the most frequently inactivated tumor suppressors in human cancers, serving as a critical negative regulator of phosphatidylinositol 3-kinase (PI3K)-AKT signaling. Although genetic mutation or deletion commonly underlie functional PTEN loss, accumulating evidence indicates that post-transcriptional and post-translational mechanisms also substantially contribute to PTEN suppression. Phosphatases of regenerating liver (PRLs), comprising PRL1, PRL2, and PRL3, are oncogenic phosphatases frequently overexpressed in both solid and hematological malignancies. Emerging studies reveal that PRLs can downregulate PTEN through a post-translational mechanism by direct dephosphorylation of PTEN at Tyr336, therefore promoting PTEN ubiquitination and proteasomal degradation. PRLs can also reduce PTEN expression through a post-transcriptional mechanism by dephosphorylating the inhibitory Tyr570 in JAK2, thereby activating the JAK2/STAT3-mediated miR-21 expression. These coordinated actions collectively amplify PI3K-AKT signaling, consequently promoting proliferation, survival, and metastasis. In the present review, we synthesize current knowledge of PRL structure, evolution, and functional diversity, evaluate genetic, biochemical, and organismal evidence linking PRLs to PTEN regulation, and discuss insights on PRL oncogenicity derived from experimental models. We further examine context-dependent functions of PRLs, unresolved questions regarding catalytic versus scaffold activities, and the therapeutic potential of targeting the PRL-PTEN axis. Understanding how PRLs modulate PTEN activity may reveal new strategies to restore tumor suppressor function in PTEN-deficient cancers. - Source: PubMed
Abou-Shanab Ahmed MYu JingmeiBai YunpengZhang Zhong-Yin - Ovarian cancer (OC) has the highest mortality rate of all gynaecological malignancies, partly attributable to its propensity for chemotherapy resistance. The most common subtype of OC is serous, of which high-grade serous ovarian cancer (HGSOC) is the most lethal subtype. Protein tyrosine phosphatase 4A3 (PTP4A3) overexpression is implicated in tumour cell invasion and metastasis by upregulating the PI3K/Akt/mTORC1 axis. Previously, we reported that PTP4A3 increased the survival of non-serous OC cells by activating the autophagy pathway. Here, we investigated the impact of PTP4A3 on cell proliferation, autophagy and chemoresistance in HGSOC cells and whether targeting PTP4A3 in HGSOC cells that overexpress this phosphatase would sensitise them to existing chemotherapeutic drugs. Gene silencing of PTP4A3 resulted in the upregulation of compensatory mechanisms that overcame the loss of PTP4A3 expression, but this was mitigated by pan-PTP4A inhibition with JMS-053 in HGSOC cells. Moreover, shRNA-mediated silencing of PTP4A3 sensitised HGSOC cells to clinically relevant chemotherapeutic drugs. Overall, we show that compensatory mechanisms from PTP4A1 and PTP4A2 can arise when specifically targeting PTP4A3 in HGSOC and that pan-PTP4A inhibition can overcome those effects. - Source: PubMed
Publication date: 2025/07/14
López-Garza AnaJames DavidCreagh EmmaMurray James T - Phosphatase of regenerating liver (PRL) family proteins, also known as protein tyrosine phosphatase 4A (PTP4A), have been implicated in many types of cancers. The PRL family of phosphatases consists of three members, PRL1, PRL2, and PRL3. PRLs have been shown to harbor oncogenic potentials and are highly expressed in a variety of cancers. Given their roles in cancer progression and metastasis, PRLs are potential targets for anticancer therapies. However, additional studies are needed to be performed to fully understand the roles of PRLs in blood cancers. - Source: PubMed
Publication date: 2024/04/26
Xiao ShiyuChen HongxiaBai YunpengZhang Zhong-YinLiu Yan - Phosphatases of regenerating liver (PRL-1, PRL-2, PRL-3; also known as PTP4A1, PTP4A2, PTP4A3, respectively) control intracellular magnesium levels by interacting with the CNNM magnesium transport regulators. Still, the exact mechanism governing magnesium transport by this protein complex is not well understood. Herein, we have developed a genetically encoded intracellular magnesium-specific reporter and demonstrate that the CNNM family inhibits the function of the TRPM7 magnesium channel. We show that the small GTPase ARL15 increases CNNM3/TRPM7 protein complex formation to reduce TRPM7 activity. Conversely, PRL-2 overexpression counteracts ARL15 binding to CNNM3 and enhances the function of TRPM7 by preventing the interaction between CNNM3 and TRPM7. Moreover, while TRPM7-induced cell signaling is promoted by PRL-1/2, it is reduced when CNNM3 is overexpressed. Lowering cellular magnesium levels reduces the interaction of CNNM3 with TRPM7 in a PRL-dependent manner, whereby knockdown of PRL-1/2 restores the protein complex formation. Cotargeting of TRPM7 and PRL-1/2 alters mitochondrial function and sensitizes cells to metabolic stress induced by magnesium depletion. These findings reveal the dynamic regulation of TRPM7 function in response to PRL-1/2 levels, to coordinate magnesium transport and reprogram cellular metabolism. - Source: PubMed
Publication date: 2023/03/27
Hardy SergeZolotarov YevgenColeman JacobRoitman SimonKhursheed HiraAubry IsabelleUetani NorikoTremblay Michel L - Phosphatases of regenerating liver (PRL-1, PRL-2, and PRL-3, also known as PTP4A1, PTP4A2, and PTP4A3) control magnesium homeostasis through an association with the CNNM magnesium transport regulators. Although high PRL levels have been linked to cancer progression, regulation of their expression is poorly understood. Here we show that modulating intracellular magnesium levels correlates with a rapid change of PRL expression by a mechanism involving its 5'UTR mRNA region. Mutations or CRISPR-Cas9 targeting of the conserved upstream ORF present in the mRNA leader derepress PRL protein synthesis and attenuate the translational response to magnesium levels. Mechanistically, magnesium depletion reduces intracellular ATP but up-regulates PRL protein expression via activation of the AMPK/mTORC2 pathway, which controls cellular energy status. Hence, altered PRL-2 expression leads to metabolic reprogramming of the cells. These findings uncover a magnesium-sensitive mechanism controlling PRL expression, which plays a role in cellular bioenergetics. - Source: PubMed
Publication date: 2019/02/04
Hardy SergeKostantin ElieWang Shan JinHristova TzvetenaGalicia-Vázquez GabrielaBaranov Pavel VPelletier JerryTremblay Michel L