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Article: SALL Proteins; Common and Antagonistic Roles in Cancer.

Álvarez, Claudia / Quiroz, Aracelly / Benítez-Riquelme, Diego / Riffo, Elizabeth / Castro, Ariel F / Pincheira, Roxana

2021 Volume 13, Issue 24

Abstract: SALL proteins are a family of four conserved C2H2 zinc finger transcription factors that play critical roles in organogenesis during embryonic development. They regulate cell proliferation, survival, migration, and stemness; consequently, they are ... ...

Abstract	SALL proteins are a family of four conserved C2H2 zinc finger transcription factors that play critical roles in organogenesis during embryonic development. They regulate cell proliferation, survival, migration, and stemness; consequently, they are involved in various human genetic disorders and cancer. SALL4 is a well-recognized oncogene; however, SALL1-3 play dual roles depending on the cancer context and stage of the disease. Current reviews of SALLs have focused only on SALL2 or SALL4, lacking an integrated view of the SALL family members in cancer. Here, we update the recent advances of the SALL members in tumor development, cancer progression, and therapy, highlighting the synergistic and/or antagonistic functions they perform in similar cancer contexts. We identified common regulatory mechanisms, targets, and signaling pathways in breast, brain, liver, colon, blood, and HPV-related cancers. In addition, we discuss the potential of the SALL family members as cancer biomarkers and in the cancer cells' response to therapies. Understanding SALL proteins' function and relationship will open new cancer biology, clinical research, and therapy perspectives.
Language	English
Publishing date	2021-12-15
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2527080-1
ISSN	2072-6694
ISSN	2072-6694
DOI	10.3390/cancers13246292
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Article: The Sall2 transcription factor promotes cell migration regulating focal adhesion turnover and integrin β1 expression.

Riffo, Elizabeth / Palma, Mario / Hepp, Matías I / Benítez-Riquelme, Diego / Torres, Vicente A / Castro, Ariel F / Pincheira, Roxana

Frontiers in cell and developmental biology

2022 Volume 10, Page(s) 1031262

Abstract: SALL2/Sall2 is a transcription factor associated with development, neuronal differentiation, and cancer. Interestingly, ...

Abstract	SALL2/Sall2 is a transcription factor associated with development, neuronal differentiation, and cancer. Interestingly,
Language	English
Publishing date	2022-11-09
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2737824-X
ISSN	2296-634X
ISSN	2296-634X
DOI	10.3389/fcell.2022.1031262
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Article: Cytosolic NUAK1 Enhances ATP Production by Maintaining Proper Glycolysis and Mitochondrial Function in Cancer Cells.

Escalona, Emilia / Muñoz, Marcelo / Pincheira, Roxana / Elorza, Álvaro A / Castro, Ariel F

Frontiers in oncology

2020 Volume 10, Page(s) 1123

Abstract: NUAK1 is an AMPK-related kinase located in the cytosol and the nucleus, whose expression associates with tumor malignancy and poor patient prognosis in several cancers. Accordingly, NUAK1 was associated with metastasis because it promotes cell migration ... ...

Abstract	NUAK1 is an AMPK-related kinase located in the cytosol and the nucleus, whose expression associates with tumor malignancy and poor patient prognosis in several cancers. Accordingly, NUAK1 was associated with metastasis because it promotes cell migration and invasion in different cancer cells. Besides, NUAK1 supports cancer cell survival under metabolic stress and maintains ATP levels in hepatocarcinoma cells, suggesting a role in energy metabolism in cancer. However, the underlying mechanism for this metabolic function, as well as its link to NUAK1 subcellular localization, is unclear. We demonstrated that cytosolic NUAK1 increases ATP levels, which associates with increased mitochondrial respiration, supporting that cytosolic NUAK1 is involved in mitochondrial function regulation in cancer cells. NUAK1 inhibition led to the formation of "donut-like" structures, providing evidence of NUAK1-dependent mitochondrial morphology regulation. Additionally, our results indicated that cytosolic NUAK1 increases the glycolytic capacity of cancer cells under mitochondrial inhibition. Nuclear NUAK1 seems to be involved in the metabolic switch to glycolysis. Altogether, our results suggest that cytosolic NUAK1 participates in mitochondrial ATP production and the maintenance of proper glycolysis in cancer cells. Our current studies support the role of NUAK1 in bioenergetics, mitochondrial homeostasis, glycolysis and metabolic capacities. They suggest different metabolic outcomes depending on its subcellular localization. The identified roles of NUAK1 in cancer metabolism provide a potential mechanism relevant for tumor progression and its association with poor patient prognosis in several cancers. Further studies could shed light on the molecular mechanisms involved in the identified metabolic NUAK1 functions.
Language	English
Publishing date	2020-07-10
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2649216-7
ISSN	2234-943X
ISSN	2234-943X
DOI	10.3389/fonc.2020.01123
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Article: NUAK1 coordinates growth factor-dependent activation of mTORC2 and Akt signaling.

Palma, Mario / Riffo, Elizabeth / Farias, Alejandro / Coliboro-Dannich, Viviana / Espinoza-Francine, Luis / Escalona, Emilia / Amigo, Roberto / Gutiérrez, José L / Pincheira, Roxana / Castro, Ariel F

Cell & bioscience

2023 Volume 13, Issue 1, Page(s) 232

Abstract: Background: mTORC2 is a critical regulator of cytoskeleton organization, cell proliferation, and cancer cell survival. Activated mTORC2 induces maximal activation of Akt by phosphorylation of Ser-473, but regulation of Akt activity and signaling ... ...

Abstract	Background: mTORC2 is a critical regulator of cytoskeleton organization, cell proliferation, and cancer cell survival. Activated mTORC2 induces maximal activation of Akt by phosphorylation of Ser-473, but regulation of Akt activity and signaling crosstalk upon growth factor stimulation are still unclear. Results: We identified that NUAK1 regulates growth factor-dependent activation of Akt by two mechanisms. NUAK1 interacts with mTORC2 components and regulates mTORC2-dependent activation of Akt by controlling lysosome positioning and mTOR association with this organelle. A second mechanism involves NUAK1 directly phosphorylating Akt at Ser-473. The effect of NUAK1 correlated with a growth factor-dependent activation of specific Akt substrates. NUAK1 induced the Akt-dependent phosphorylation of FOXO1/3a (Thr-24/Thr-32) but not of TSC2 (Thr-1462). According to a subcellular compartmentalization that could explain NUAK1's differential effect on the Akt substrates, we found that NUAK1 is associated with early endosomes but not with plasma membrane, late endosomes, or lysosomes. NUAK1 was required for the Akt/FOXO1/3a axis, regulating p21CIP1, p27KIP1, and FoxM1 expression and cancer cell survival upon EGFR stimulation. Pharmacological inhibition of NUAK1 potentiated the cell death effect induced by Akt or mTOR pharmacological blockage. Analysis of human tissue data revealed that NUAK1 expression positively correlates with EGFR expression and Akt Ser-473 phosphorylation in several human cancers. Conclusions: Our results showed that NUAK1 kinase controls mTOR subcellular localization and induces Akt phosphorylation, demonstrating that NUAK1 regulates the growth factor-dependent activation of Akt signaling. Therefore, targeting NUAK1, or co-targeting it with Akt or mTOR inhibitors, may be effective in cancers with hyperactivated Akt signaling.
Language	English
Publishing date	2023-12-22
Publishing country	England
Document type	Journal Article
ZDB-ID	2593367-X
ISSN	2045-3701
ISSN	2045-3701
DOI	10.1186/s13578-023-01185-2
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Article: Characterization of

Farkas, Carlos / Quiroz, Aracelly / Alvarez, Claudia / Hermosilla, Viviana / Aylwin, Carlos F / Lomniczi, Alejandro / Castro, Ariel F / Hepp, Matias I / Pincheira, Roxana

Frontiers in genetics

2021 Volume 12, Page(s) 613808

Abstract: The SALL2 transcription factor, an evolutionarily conserved gene through vertebrates, is involved in normal development and neuronal differentiation. In disease, SALL2 is associated with eye, kidney, and brain disorders, but mainly is related to cancer. ... ...

Abstract	The SALL2 transcription factor, an evolutionarily conserved gene through vertebrates, is involved in normal development and neuronal differentiation. In disease, SALL2 is associated with eye, kidney, and brain disorders, but mainly is related to cancer. Some studies support a tumor suppressor role and others an oncogenic role for SALL2, which seems to depend on the cancer type. An additional consideration is tissue-dependent expression of different SALL2 isoforms. Human and mouse
Language	English
Publishing date	2021-02-22
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2606823-0
ISSN	1664-8021
ISSN	1664-8021
DOI	10.3389/fgene.2021.613808
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Article ; Online: DISC1 promotes translation maintenance during sodium arsenite-induced oxidative stress.

Fuentes-Villalobos, Francisco / Farkas, Carlos / Riquelme-Barrios, Sebastián / Armijo, Marisol E / Soto-Rifo, Ricardo / Pincheira, Roxana / Castro, Ariel F

Biochimica et biophysica acta. Gene regulatory mechanisms

2019 Volume 1862, Issue 6, Page(s) 657–669

Abstract: Variation in Disrupted-in-Schizophrenia 1 (DISC1) increases the risk for neurodegenerative diseases, schizophrenia, and other mental disorders. However, the functions of DISC1 associated with the development of these diseases remain unclear. DISC1 has ... ...

Abstract	Variation in Disrupted-in-Schizophrenia 1 (DISC1) increases the risk for neurodegenerative diseases, schizophrenia, and other mental disorders. However, the functions of DISC1 associated with the development of these diseases remain unclear. DISC1 has been reported to inhibit Akt/mTORC1 signaling, a major regulator of translation, and recent studies indicate that DISC1 could exert a direct role in translational regulation. Here, we present evidence of a novel role of DISC1 in the maintenance of protein synthesis during oxidative stress. In order to investigate DISC1 function independently of Akt/mTORC1, we used Tsc2-/- cells, where mTORC1 activation is independent of Akt. DISC1 knockdown enhanced inhibition of protein synthesis in cells treated with sodium arsenite (SA), an oxidative agent used for studying stress granules (SGs) dynamics and translational control. N-acetyl-cysteine inhibited the effect of DISC1, suggesting that DISC1 affects translation in response to oxidative stress. DISC1 decreased SGs number in SA-treated cells, but resided outside SGs and maintained protein synthesis independently of a proper SG nucleation. DISC1-dependent stimulation of translation in SA-treated cells was supported by its interaction with eIF3h, a component of the canonical translation initiation machinery. Consistent with a role in the homeostatic maintenance of translation, DISC1 knockdown or overexpression decreased cell viability after SA exposure. Our data suggest that DISC1 is a relevant component of the cellular response to stress, maintaining certain levels of translation and preserving cell integrity. This novel function of DISC1 might be involved in its association with pathologies affecting tissues frequently exposed to oxidative stress.
MeSH term(s)	Animals ; Arsenites/pharmacology ; Cell Survival/drug effects ; Cytoplasmic Granules/metabolism ; DNA Helicases/metabolism ; Eukaryotic Initiation Factor-3/metabolism ; Gene Expression Regulation ; Gene Knockdown Techniques ; HEK293 Cells ; Humans ; Mechanistic Target of Rapamycin Complex 1 ; Mice ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Oncogene Protein v-akt ; Oxidative Stress/drug effects ; Poly-ADP-Ribose Binding Proteins/metabolism ; RNA Helicases/metabolism ; RNA Recognition Motif Proteins/metabolism ; Sodium Compounds/pharmacology ; Transcriptome ; Tuberous Sclerosis Complex 2 Protein/genetics
Chemical Substances	Arsenites ; DISC1 protein, human ; Eukaryotic Initiation Factor-3 ; Nerve Tissue Proteins ; Poly-ADP-Ribose Binding Proteins ; RNA Recognition Motif Proteins ; Sodium Compounds ; TSC2 protein, human ; Tuberous Sclerosis Complex 2 Protein ; sodium arsenite (48OVY2OC72) ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1) ; Oncogene Protein v-akt (EC 2.7.11.1) ; DNA Helicases (EC 3.6.4.-) ; G3BP1 protein, human (EC 3.6.4.12) ; RNA Helicases (EC 3.6.4.13)
Language	English
Publishing date	2019-05-07
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2918786-2
ISSN	1876-4320 ; 1874-9399
ISSN (online)	1876-4320
ISSN	1874-9399
DOI	10.1016/j.bbagrm.2019.05.001
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Article ; Online: Identification of a nuclear localization signal and importin beta members mediating NUAK1 nuclear import inhibited by oxidative stress.

Palma, Mario / Riffo, Elizabeth N / Suganuma, Tamaki / Washburn, Michael P / Workman, Jerry L / Pincheira, Roxana / Castro, Ariel F

Journal of cellular biochemistry

2019 Volume 120, Issue 9, Page(s) 16088–16107

Abstract: NUAK1 is a serine/threonine kinase member of the AMPK-α family. NUAK1 regulates several processes in tumorigenesis; however, its regulation and molecular targets are still poorly understood. Bioinformatics analysis predicted that the majority of NUAK1 ... ...

Abstract	NUAK1 is a serine/threonine kinase member of the AMPK-α family. NUAK1 regulates several processes in tumorigenesis; however, its regulation and molecular targets are still poorly understood. Bioinformatics analysis predicted that the majority of NUAK1 localizes in the nucleus. However, there are no studies about the regulation of NUAK1 subcellular distribution. Here, we analyzed NUAK1 localization in several human cell lines, mouse embryo fibroblasts, and normal mouse tissues. We found that NUAK1 is located in the nucleus and also in the cytoplasm. Through bioinformatics analysis and studies comparing subcellular localization of wild type and NUAK1 mutants, we identified a conserved bipartite nuclear localization signal at the N-terminal domain of NUAK1. Based on mass spectrometry analysis, we found that NUAK1 interacts with importin-β members including importin-β1 (KPNB1), importin-7 (IPO7), and importin-9 (IPO9). We confirmed that importin-β members are responsible for NUAK1 nuclear import through the inhibition of importin-β by Importazole and the knockdown of either IPO7 or IPO9. In addition, we found that oxidative stress induces NUAK1 cytoplasmic accumulation, indicating that oxidative stress affects NUAK1 nuclear transport. Thus, our study is the first evidence of an active nuclear transport mechanism regulating NUAK1 subcellular localization. These data will lead to investigations of the molecular targets of NUAK1 according to its subcellular distribution, which could be new biomarkers or targets for cancer therapies.
MeSH term(s)	Active Transport, Cell Nucleus ; Animals ; Cell Line ; Cytoplasm/metabolism ; HCT116 Cells ; HEK293 Cells ; HeLa Cells ; Humans ; MCF-7 Cells ; Mice ; Nuclear Localization Signals/metabolism ; Oxidative Stress ; Protein Kinases/genetics ; Protein Kinases/metabolism ; Repressor Proteins/genetics ; Repressor Proteins/metabolism ; beta Karyopherins/metabolism
Chemical Substances	Nuclear Localization Signals ; Repressor Proteins ; beta Karyopherins ; Protein Kinases (EC 2.7.-) ; NUAK1 protein, human (EC 2.7.1.-) ; NUAK1 protein, mouse (EC 2.7.1.-)
Language	English
Publishing date	2019-05-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	392402-6
ISSN	1097-4644 ; 0730-2312
ISSN (online)	1097-4644
ISSN	0730-2312
DOI	10.1002/jcb.28890
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Article: A Trichostatin A (TSA)/Sp1-mediated mechanism for the regulation of SALL2 tumor suppressor in Jurkat T cells.

Hepp, Matías I / Escobar, David / Farkas, Carlos / Hermosilla, Viviana E / Álvarez, Claudia / Amigo, Roberto / Gutiérrez, José L / Castro, Ariel F / Pincheira, Roxana

Biochimica et biophysica acta. Gene regulatory mechanisms

2018

Abstract: SALL2 is a transcription factor involved in development and disease. Deregulation of SALL2 has been associated with cancer, suggesting that it plays a role in the disease. However, how SALL2 is regulated and why is deregulated in cancer remain poorly ... ...

Abstract	SALL2 is a transcription factor involved in development and disease. Deregulation of SALL2 has been associated with cancer, suggesting that it plays a role in the disease. However, how SALL2 is regulated and why is deregulated in cancer remain poorly understood. We previously showed that the p53 tumor suppressor represses SALL2 under acute genotoxic stress. Here, we investigated the effect of Histone Deacetylase Inhibitor (HDACi) Trichostatin A (TSA), and involvement of Sp1 on expression and function of SALL2 in Jurkat T cells. We show that SALL2 mRNA and protein levels were enhanced under TSA treatment. Both, TSA and ectopic expression of Sp1 transactivated the SALL2 P2 promoter. This transactivation effect was blocked by the Sp1-binding inhibitor mithramycin A. Sp1 bound in vitro and in vivo to the proximal region of the P2 promoter. TSA induced Sp1 binding to the P2 promoter, which correlated with dynamic changes on H4 acetylation and concomitant recruitment of p300 or HDAC1 in a mutually exclusive manner. Our results suggest that TSA-induced Sp1-Lys703 acetylation contributes to the transcriptional activation of the P2 promoter. Finally, using a CRISPR/Cas9 SALL2-KO Jurkat-T cell model and gain of function experiments, we demonstrated that SALL2 upregulation is required for TSA-mediated cell death. Thus, our study identified Sp1 as a novel transcriptional regulator of SALL2, and proposes a novel epigenetic mechanism for SALL2 regulation in Jurkat-T cells. Altogether, our data support SALL2 function as a tumor suppressor, and SALL2 involvement in cell death response to HDACi.
Language	English
Publishing date	2018-05-18
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 1874-9399 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	1874-9399 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439
DOI	10.1016/j.bbagrm.2018.05.002
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Article ; Online: Consequences of interrupted Rheb-to-AMPK feedback signaling in tuberous sclerosis complex and cancer.

Lacher, Markus D / Pincheira, Roxana J / Castro, Ariel F

Small GTPases

2011 Volume 2, Issue 4, Page(s) 211–216

Abstract: Rheb is a small GTPase primarily known for activating mammalian target of rapamycin complex 1 (mTORC1) and promoting cell growth in response to insulin and nutrients (amino acids, glucose). Shortage of glucose activates adenosine 5'-monophosphate- ... ...

Abstract	Rheb is a small GTPase primarily known for activating mammalian target of rapamycin complex 1 (mTORC1) and promoting cell growth in response to insulin and nutrients (amino acids, glucose). Shortage of glucose activates adenosine 5'-monophosphate-activated protein kinase (AMPK), which induces catabolic processes that produce ATP and suppresses energy-consuming anabolic reactions. As part of the latter response, AMPK activates the TSC1-TSC2 tumor suppressor complex, which in turn inhibits Rheb, thereby reducing mTORC1 activity and consequently suppressing protein synthesis. We recently identified an mTORC1-independent Rheb-to-AMPK feedback signaling loop in Tsc2-null in vitro models of Tuberous Sclerosis Complex (TSC). In addition to activating AMPK, Rheb reduced the nuclear levels of the cyclin-dependent kinase inhibitor p27(KIP1) (p27). Importantly, Rheb-mediated repression of p27 correlated with activation of Cdk2 and cell proliferation, and with tumor formation by TSC cells. Considering that AMPK was previously reported to regulate stability and subcellular localization of p27, we hypothesize that Rheb regulates p27 in TSC cells by activating AMPK. This article discusses how Rheb-to-AMPK, and p27 signaling may impact on disease progression and treatment of TSC, including sporadic lymphangioleiomyomatosis (S-LAM) and malignancies.
Language	English
Publishing date	2011-07-01
Publishing country	United States
Document type	Journal Article
ZDB-ID	2682247-7
ISSN	2154-1256 ; 2154-1248
ISSN (online)	2154-1256
ISSN	2154-1248
DOI	10.4161/sgtp.2.4.16703
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Article ; Online: Developmental SALL2 transcription factor: a new player in cancer.

Hermosilla, Viviana E / Hepp, Matias I / Escobar, David / Farkas, Carlos / Riffo, Elizabeth N / Castro, Ariel F / Pincheira, Roxana

Carcinogenesis

2017 Volume 38, Issue 7, Page(s) 680–690

Abstract: SALL2, also known as Spalt-like transcription factor 2, is a member of the SALL family of transcription factors involved in development and conserved through evolution. Since its identification in 1996, findings indicate that SALL2 plays a role in ... ...

Abstract	SALL2, also known as Spalt-like transcription factor 2, is a member of the SALL family of transcription factors involved in development and conserved through evolution. Since its identification in 1996, findings indicate that SALL2 plays a role in neurogenesis, neuronal differentiation and eye development. Consistently, SALL2 deficiency associates with neural tube defects and coloboma, a congenital eye disease. Relevant to cancer, clinical studies indicate that SALL2 is deregulated in various cancers and is a specific biomarker for Synovial Sarcoma. However, the significance of SALL2 deregulation in this disease is controversial. Here, we present and discuss all available information about SALL2 since its discovery, including isoforms, regulation, targets and functions. We specifically discuss the role of SALL2 in the regulation of cell proliferation and survival within the context of the identified target genes, its interaction with viral oncogenes, and its association with the TP53 tumor suppressor and MYC oncogene. Special attention is given to p53-independent SALL2 regulation of pro-apoptotic genes BAX and PMAIP1, and the implication of these findings on the apoptotic response of cancer cells to therapy. Understanding SALL2 function and the molecular mechanisms governing its expression and activity is critical to comprehend why and how SALL2 could contribute to disease. This knowledge will open new perspectives for the development of molecular targeted approaches in disease.
MeSH term(s)	Apoptosis/genetics ; Biomarkers, Tumor/biosynthesis ; Biomarkers, Tumor/genetics ; Gene Expression Regulation, Neoplastic ; Humans ; Neoplasms/genetics ; Neoplasms/pathology ; Proto-Oncogene Proteins c-bcl-2/genetics ; Transcription Factors/biosynthesis ; Transcription Factors/genetics ; Tumor Suppressor Protein p53/genetics ; bcl-2-Associated X Protein/genetics
Chemical Substances	Biomarkers, Tumor ; PMAIP1 protein, human ; Proto-Oncogene Proteins c-bcl-2 ; SALL2 protein, human ; Transcription Factors ; Tumor Suppressor Protein p53 ; bcl-2-Associated X Protein
Language	English
Publishing date	2017-07-01
Publishing country	England
Document type	Journal Article
ZDB-ID	603134-1
ISSN	1460-2180 ; 0143-3334
ISSN (online)	1460-2180
ISSN	0143-3334
DOI	10.1093/carcin/bgx036
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