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Article ; Online: Ca

Sayedyahossein, Samar / Thines, Louise / Sacks, David B

2023 Volume 110, Page(s) 110846

Abstract: The Hippo signaling pathway is a master regulator of organ size and tissue homeostasis. Hippo integrates a broad range of cellular signals to regulate numerous processes, such as cell proliferation, differentiation, migration and mechanosensation. ... ...

Abstract	The Hippo signaling pathway is a master regulator of organ size and tissue homeostasis. Hippo integrates a broad range of cellular signals to regulate numerous processes, such as cell proliferation, differentiation, migration and mechanosensation. Ca
MeSH term(s)	Hippo Signaling Pathway ; Protein Serine-Threonine Kinases/metabolism ; Signal Transduction/physiology ; Cell Proliferation/physiology ; Cell Differentiation
Chemical Substances	Protein Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2023-08-06
Publishing country	England
Document type	Review ; Journal Article
ZDB-ID	1002702-6
ISSN	1873-3913 ; 0898-6568
ISSN (online)	1873-3913
ISSN	0898-6568
DOI	10.1016/j.cellsig.2023.110846
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Zs.A 2579: Show issues

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Article ; Online: Disruption of Ca

Thines, Louise / Jang, Hyunbum / Li, Zhigang / Sayedyahossein, Samar / Maloney, Ryan / Nussinov, Ruth / Sacks, David B

Protein science : a publication of the Protein Society

2024 Volume 33, Issue 5, Page(s) e4982

Abstract: KSR1, a key scaffold protein for the MAPK pathway, facilitates ERK activation upon growth factor stimulation. We recently demonstrated that KSR1 binds the ... ...

Abstract	KSR1, a key scaffold protein for the MAPK pathway, facilitates ERK activation upon growth factor stimulation. We recently demonstrated that KSR1 binds the Ca
MeSH term(s)	Calmodulin/chemistry ; Calcium Signaling ; Protein Binding ; Mutation ; Mutagenesis, Site-Directed ; Calcium/metabolism
Chemical Substances	Calmodulin ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2024-04-09
Publishing country	United States
Document type	Journal Article
ZDB-ID	1106283-6
ISSN	1469-896X ; 0961-8368
ISSN (online)	1469-896X
ISSN	0961-8368
DOI	10.1002/pro.4982
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Zs.A 3407: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Calmodulin activates the Hippo signaling pathway by promoting LATS1 kinase-mediated inhibitory phosphorylation of the transcriptional coactivator YAP.

Thines, Louise / Gorisse, Laëtitia / Li, Zhigang / Sayedyahossein, Samar / Sacks, David B

The Journal of biological chemistry

2022 Volume 298, Issue 5, Page(s) 101839

Abstract: The Hippo signaling pathway regulates tissue growth and cell fate, and its dysregulation can induce tumorigenesis. When Hippo is activated by cell-cell contact, extracellular signals, or cell polarity among others, the large tumor suppressor 1 (LATS1) ... ...

Abstract	The Hippo signaling pathway regulates tissue growth and cell fate, and its dysregulation can induce tumorigenesis. When Hippo is activated by cell-cell contact, extracellular signals, or cell polarity among others, the large tumor suppressor 1 (LATS1) kinase catalyzes inhibitory phosphorylation of the transcriptional coactivator Yes-associated protein (YAP) to maintain YAP in the cytoplasm or promote its degradation. Separately, calmodulin is a Ca
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Calmodulin/metabolism ; Cell Proliferation/physiology ; Hippo Signaling Pathway ; Mammals/metabolism ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; Phosphorylation ; Protein Serine-Threonine Kinases/genetics ; Transcription Factors/genetics ; Transcription Factors/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Calmodulin ; Phosphoproteins ; Transcription Factors ; Protein Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2022-03-17
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2022.101839
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Article ; Online: Insulin suppresses transcriptional activity of yes-associated protein in insulin target cells.

Sayedyahossein, Samar / Hedman, Andrew C / Sacks, David B

Molecular biology of the cell

2019 Volume 31, Issue 2, Page(s) 131–141

Abstract: Yes-associated protein (YAP), the main transcriptional coactivator of the Hippo pathway, integrates multiple inputs from different signaling cascades. Evidence implicates YAP in the control of cellular nutrient and energy status, but the underlying ... ...

Abstract	Yes-associated protein (YAP), the main transcriptional coactivator of the Hippo pathway, integrates multiple inputs from different signaling cascades. Evidence implicates YAP in the control of cellular nutrient and energy status, but the underlying mechanisms are not fully elucidated. Here we show that insulin modulates YAP transcriptional activity in classic insulin target cells, namely HepG2 and C2C12. Insulin increases YAP phosphorylation and significantly decreases YAP abundance in HepG2 cell nuclei. Proximity ligation assay analysis revealed a marked reduction in the interaction of YAP with TEA domain (TEAD) transcription factors in the nuclei of insulin-exposed cells. Consistent with these findings, insulin impaired both YAP/TEAD-mediated transcription and transcription of YAP target genes in HepG2 and C2C12 cells. Serum starvation abrogated the effect of insulin on YAP phosphorylation and YAP transcription. Both the expression of two gluconeogenesis genes, G6PC and PCK1, and the inhibitory effect of insulin on these genes were attenuated in YAP-deficient HepG2 cells. Our results identify insulin as a previously undescribed suppressor of YAP activity in insulin target cells and provide insight into cross-talk between the insulin and Hippo pathways.
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Cell Cycle Proteins/metabolism ; Cell Line ; Cell Nucleus/metabolism ; DNA-Binding Proteins/metabolism ; Hep G2 Cells ; Humans ; Insulin/metabolism ; Insulin/physiology ; Intracellular Signaling Peptides and Proteins/metabolism ; Phosphoproteins/metabolism ; Phosphorylation ; Signal Transduction ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Transcriptional Activation/drug effects
Chemical Substances	Adaptor Proteins, Signal Transducing ; Cell Cycle Proteins ; DNA-Binding Proteins ; Insulin ; Intracellular Signaling Peptides and Proteins ; Phosphoproteins ; Transcription Factors ; YAP1 protein, human
Language	English
Publishing date	2019-11-06
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E19-04-0205
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Zs.A 2853: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: PANX3 Channels Regulate Architecture, Adhesion, Barrier Function, and Inflammation in the Skin.

O'Donnell, Brooke L / Sanchez-Pupo, Rafael E / Sayedyahossein, Samar / Karimi, Mehdi / Bahmani, Mehrnoosh / Zhang, Christopher / Johnston, Danielle / Kelly, John J / Wakefield, C Brent / Barr, Kevin / Dagnino, Lina / Penuela, Silvia

The Journal of investigative dermatology

2023 Volume 143, Issue 8, Page(s) 1509–1519.e14

Abstract: The channel-forming glycoprotein PANX3 functions in cutaneous wound healing and keratinocyte differentiation, but its role in maintaining skin homeostasis through aging is not yet understood. We found that PANX3 is absent in newborn skin but becomes ... ...

Abstract	The channel-forming glycoprotein PANX3 functions in cutaneous wound healing and keratinocyte differentiation, but its role in maintaining skin homeostasis through aging is not yet understood. We found that PANX3 is absent in newborn skin but becomes upregulated with age. We characterized the skin of global Panx3-knockout (KO) mice and found that KO dorsal skin showed sex differences at different ages but generally had reduced dermal and hypodermal areas compared with age-matched controls. Transcriptomic analysis of the KO epidermis revealed reduced E-cadherin stabilization and Wnt signaling compared with that of wild-type, consistent with the inability of primary KO keratinocytes to adhere in culture and diminished epidermal barrier function in KO mice. We also observed increased inflammatory signaling in the KO epidermis and a higher incidence of dermatitis in aged KO mice compared with that in wild-type controls. These findings suggest that during skin aging, PANX3 is critical in the maintenance of dorsal skin architecture, keratinocyte cell-cell and cell-matrix adhesion, and inflammatory skin responses.
MeSH term(s)	Mice ; Animals ; Female ; Male ; Skin ; Keratinocytes/physiology ; Epidermis ; Inflammation/genetics ; Wnt Signaling Pathway ; Mice, Knockout
Language	English
Publishing date	2023-02-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80136-7
ISSN	1523-1747 ; 0022-202X
ISSN (online)	1523-1747
ISSN	0022-202X
DOI	10.1016/j.jid.2023.01.030
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Article ; Online: Discovery of small molecule inhibitors that effectively disrupt IQGAP1-Cdc42 interaction in breast cancer cells.

Sayedyahossein, Samar / Smith, Jessica / Barnaeva, Elena / Li, Zhigang / Choe, Jun / Ronzetti, Michael / Dextras, Christopher / Hu, Xin / Marugan, Juan / Southall, Noel / Baljinnyam, Bolormaa / Thines, Louise / Tran, Andy D / Ferrer, Marc / Sacks, David B

Scientific reports

2022 Volume 12, Issue 1, Page(s) 17372

Abstract: The small GTPase Cdc42 is an integral component of the cytoskeleton, and its dysregulation leads to pathophysiological conditions, such as cancer. Binding of Cdc42 to the scaffold protein IQGAP1 stabilizes Cdc42 in its active form. The interaction ... ...

Abstract	The small GTPase Cdc42 is an integral component of the cytoskeleton, and its dysregulation leads to pathophysiological conditions, such as cancer. Binding of Cdc42 to the scaffold protein IQGAP1 stabilizes Cdc42 in its active form. The interaction between Cdc42 and IQGAP1 enhances migration and invasion of cancer cells. Disrupting this association could impair neoplastic progression and metastasis; however, no effective means to achieve this has been described. Here, we screened 78,500 compounds using a homogeneous time resolved fluorescence-based assay to identify small molecules that disrupt the binding of Cdc42 to IQGAP1. From the combined results of the validation assay and counter-screens, we selected 44 potent compounds for cell-based experiments. Immunoprecipitation and cell viability analysis rendered four lead compounds, namely NCGC00131308, NCGC00098561, MLS000332963 and NCGC00138812, three of which inhibited proliferation and migration of breast carcinoma cells. Microscale thermophoresis revealed that two compounds bind directly to Cdc42. One compound reduced the amount of active Cdc42 in cells and effectively impaired filopodia formation. Docking analysis provided plausible models of the compounds binding to the hydrophobic pocket adjacent to the GTP binding site of Cdc42. In conclusion, we identified small molecules that inhibit binding between Cdc42 and IQGAP1, which could potentially yield chemotherapeutic agents.
MeSH term(s)	Breast Neoplasms/drug therapy ; Female ; Guanosine Triphosphate ; Humans ; Signal Transduction/physiology ; cdc42 GTP-Binding Protein/metabolism ; ras GTPase-Activating Proteins/metabolism
Chemical Substances	IQ motif containing GTPase activating protein 1 ; ras GTPase-Activating Proteins ; Guanosine Triphosphate (86-01-1) ; cdc42 GTP-Binding Protein (EC 3.6.5.2)
Language	English
Publishing date	2022-10-17
Publishing country	England
Document type	Journal Article
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-022-21342-w
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Article: Integrins and small GTPases as modulators of phagocytosis.

Sayedyahossein, Samar / Dagnino, Lina

International review of cell and molecular biology

2013 Volume 302, Page(s) 321–354

Abstract: Phagocytosis is the mechanism whereby cells engulf large particles. This process has long been recognized as a critical component of the innate immune response, which constitutes the organism's defense against microorganisms. In addition, phagocytic ... ...

Abstract	Phagocytosis is the mechanism whereby cells engulf large particles. This process has long been recognized as a critical component of the innate immune response, which constitutes the organism's defense against microorganisms. In addition, phagocytic internalization of apoptotic cells or cell fragments plays important roles in tissue homeostasis and remodeling. Phagocytosis requires target interactions with receptors on the plasma membrane of the phagocytic cell. Integrins have been identified as important mediators of particle clearance, in addition to their well-established roles in cell adhesion, migration and mechanotransduction. Indeed, these ubiquitously expressed proteins impart phagocytic capacity to epithelial, endothelial and mesenchymal cell types. The importance of integrins in particle internalization is emphasized by the ability of microbial and viral pathogens to exploit their signaling pathways to invade host cells, and by the wide variety of disorders that arise from abnormalities in integrin-dependent phagocytic uptake.
MeSH term(s)	Animals ; Bacterial Infections/immunology ; Bacterial Infections/metabolism ; GTP Phosphohydrolases/immunology ; GTP Phosphohydrolases/metabolism ; Homeostasis/physiology ; Humans ; Immune System Diseases/immunology ; Immune System Diseases/metabolism ; Integrins/immunology ; Integrins/metabolism ; Phagocytes/cytology ; Phagocytes/immunology ; Phagocytes/metabolism ; Phagocytosis/physiology ; Signal Transduction/immunology ; Virus Diseases/immunology ; Virus Diseases/metabolism
Chemical Substances	Integrins ; GTP Phosphohydrolases (EC 3.6.1.-)
Language	English
Publishing date	2013
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2427220-6
ISSN	1937-6448 ; 0074-7696
ISSN	1937-6448 ; 0074-7696
DOI	10.1016/B978-0-12-407699-0.00006-6
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Article ; Online: Emerging functions and clinical prospects of connexins and pannexins in melanoma.

Varela-Vázquez, Adrián / Guitián-Caamaño, Amanda / Carpintero-Fernandez, Paula / Fonseca, Eduardo / Sayedyahossein, Samar / Aasen, Trond / Penuela, Silvia / Mayán, María D

Biochimica et biophysica acta. Reviews on cancer

2020 Volume 1874, Issue 1, Page(s) 188380

Abstract: Cellular communication through gap junctions and hemichannels formed by connexins and through channels made by pannexins allows for metabolic cooperation and control of cellular activity and signalling. These channel proteins have been described to be ... ...

Abstract	Cellular communication through gap junctions and hemichannels formed by connexins and through channels made by pannexins allows for metabolic cooperation and control of cellular activity and signalling. These channel proteins have been described to be tumour suppressors that regulate features such as cell death, proliferation and differentiation. However, they display cancer type-dependent and stage-dependent functions and may facilitate tumour progression through junctional and non-junctional pathways. The accumulated knowledge and emerging strategies to target connexins and pannexins are providing novel clinical opportunities for the treatment of cancer. Here, we provide an updated overview of the role of connexins and pannexins in malignant melanoma. We discuss how targeting of these channel proteins may be used to potentiate antitumour effects in therapeutic settings, including through improved immune-mediated tumour elimination.
MeSH term(s)	Animals ; Antineoplastic Agents, Immunological/pharmacology ; Antineoplastic Agents, Immunological/therapeutic use ; Carcinogenesis/drug effects ; Carcinogenesis/immunology ; Carcinogenesis/pathology ; Cell Communication/drug effects ; Cell Communication/immunology ; Cell Line, Tumor ; Connexins/agonists ; Connexins/antagonists & inhibitors ; Connexins/metabolism ; Disease Models, Animal ; Disease Progression ; Gap Junctions/drug effects ; Gap Junctions/pathology ; Host Microbial Interactions/drug effects ; Host Microbial Interactions/immunology ; Humans ; Melanoma/drug therapy ; Melanoma/immunology ; Melanoma/mortality ; Melanoma/secondary ; Microbiota/immunology ; Neoplasm Invasiveness/immunology ; Neoplasm Invasiveness/pathology ; Neoplasm Invasiveness/prevention & control ; Neoplasm Metastasis/immunology ; Neoplasm Metastasis/pathology ; Neoplasm Metastasis/prevention & control ; Neoplasm Staging ; Signal Transduction/drug effects ; Signal Transduction/immunology ; Skin/cytology ; Skin/microbiology ; Skin/pathology ; Skin Neoplasms/drug therapy ; Skin Neoplasms/immunology ; Skin Neoplasms/mortality ; Skin Neoplasms/pathology ; Tumor Microenvironment/drug effects ; Tumor Microenvironment/immunology
Chemical Substances	Antineoplastic Agents, Immunological ; Connexins
Language	English
Publishing date	2020-05-24
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2918802-7
ISSN	1879-2561 ; 0304-419X
ISSN (online)	1879-2561
ISSN	0304-419X
DOI	10.1016/j.bbcan.2020.188380
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Article ; Online: Integrin-Linked Kinase Is Indispensable for Keratinocyte Differentiation and Epidermal Barrier Function.

Sayedyahossein, Samar / Rudkouskaya, Alena / Leclerc, Valerie / Dagnino, Lina

The Journal of investigative dermatology

2015 Volume 136, Issue 2, Page(s) 425–435

Abstract: A functional permeability barrier is essential to prevent the passage of water and electrolytes, macromolecules, and pathogens through the epidermis. This is accomplished in terminally differentiated keratinocytes through formation of a cornified ... ...

Abstract	A functional permeability barrier is essential to prevent the passage of water and electrolytes, macromolecules, and pathogens through the epidermis. This is accomplished in terminally differentiated keratinocytes through formation of a cornified envelope and the assembly of tight intercellular junctions. Integrin-linked kinase (ILK) is a scaffold protein essential for hair follicle morphogenesis and epidermal attachment to the basement membrane. However, the biological functions of ILK in differentiated keratinocytes remain poorly understood. Furthermore, whether ILK is implicated in keratinocyte differentiation and intercellular junction formation has remained an unresolved issue. Here we describe a pivotal role for ILK in keratinocyte differentiation responses to increased extracellular Ca(2+), regulation of adherens and tight junction assembly, and the formation of an outside-in permeability barrier toward macromolecules. In the absence of ILK, the calcium sensing receptor, E-cadherin, and ZO-1 fail to translocate to the cell membrane, through mechanisms that involve abnormalities in microtubules and in RhoA activation. In situ, ILK-deficient epidermis exhibits reduced tight junction formation and increased outside-in permeability to a dextran tracer, indicating reduced barrier properties toward macromolecules. Therefore, ILK is an essential component of keratinocyte differentiation programs that contribute to epidermal integrity and the establishment of its barrier properties.
MeSH term(s)	Animals ; Basement Membrane/metabolism ; Cell Differentiation/physiology ; Cell Membrane Permeability/physiology ; Cells, Cultured ; Epidermis/metabolism ; Homeostasis/physiology ; Keratinocytes/cytology ; Mice ; Mice, Inbred Strains ; Models, Animal ; Protein-Serine-Threonine Kinases/metabolism ; Receptors, Calcium-Sensing/metabolism
Chemical Substances	Receptors, Calcium-Sensing ; integrin-linked kinase (EC 2.7.1.-) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2015-11-18
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80136-7
ISSN	1523-1747 ; 0022-202X
ISSN (online)	1523-1747
ISSN	0022-202X
DOI	10.1016/j.jid.2015.10.056
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Article ; Online: Pannexin 1 binds β-catenin to modulate melanoma cell growth and metabolism.

Sayedyahossein, Samar / Huang, Kenneth / Li, Zhigang / Zhang, Christopher / Kozlov, Alexandra M / Johnston, Danielle / Nouri-Nejad, Daniel / Dagnino, Lina / Betts, Dean H / Sacks, David B / Penuela, Silvia

The Journal of biological chemistry

2021 Volume 296, Page(s) 100478

Abstract: Melanoma is the most aggressive skin malignancy with increasing incidence worldwide. Pannexin1 (PANX1), a member of the pannexin family of channel-forming glycoproteins, regulates cellular processes in melanoma cells including proliferation, migration, ... ...

Abstract	Melanoma is the most aggressive skin malignancy with increasing incidence worldwide. Pannexin1 (PANX1), a member of the pannexin family of channel-forming glycoproteins, regulates cellular processes in melanoma cells including proliferation, migration, and invasion/metastasis. However, the mechanisms responsible for coordinating and regulating PANX1 function remain unclear. Here, we demonstrated a direct interaction between the C-terminal region of PANX1 and the N-terminal portion of β-catenin, a key transcription factor in the Wnt pathway. At the protein level, β-catenin was significantly decreased when PANX1 was either knocked down or inhibited by two PANX1 blockers, Probenecid and Spironolactone. Immunofluorescence imaging showed a disrupted pattern of β-catenin localization at the cell membrane in PANX1-deficient cells, and transcription of several Wnt target genes, including MITF, was suppressed. In addition, a mitochondrial stress test revealed that the metabolism of PANX1-deficient cells was impaired, indicating a role for PANX1 in the regulation of the melanoma cell metabolic profile. Taken together, our data show that PANX1 directly interacts with β-catenin to modulate growth and metabolism in melanoma cells. These findings provide mechanistic insight into PANX1-mediated melanoma progression and may be applicable to other contexts where PANX1 and β-catenin interact as a potential new component of the Wnt signaling pathway.
MeSH term(s)	Animals ; Cell Cycle ; Cell Line, Tumor ; Cell Movement ; Cell Proliferation ; Connexins/genetics ; Connexins/metabolism ; Connexins/physiology ; Humans ; Melanoma/genetics ; Melanoma/metabolism ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Nerve Tissue Proteins/physiology ; Transcription Factors/metabolism ; Wnt Signaling Pathway ; beta Catenin/metabolism ; beta Catenin/physiology
Chemical Substances	CTNNB1 protein, human ; Connexins ; Nerve Tissue Proteins ; PANX1 protein, human ; Transcription Factors ; beta Catenin
Language	English
Publishing date	2021-02-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2021.100478
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