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Article ; Online: Nup62-mediated nuclear import of p63 in squamous cell carcinoma.

Borlido, Joana / D'Angelo, Maximiliano A

2017 Volume 19, Issue 1, Page(s) 3–4

MeSH term(s)	Active Transport, Cell Nucleus ; Biomarkers, Tumor ; Carcinoma, Squamous Cell ; Humans ; Immunohistochemistry ; Nuclear Pore Complex Proteins ; Tumor Suppressor Proteins
Chemical Substances	Biomarkers, Tumor ; Nuclear Pore Complex Proteins ; Tumor Suppressor Proteins
Language	English
Publishing date	2017-12-18
Publishing country	England
Document type	Journal Article ; Comment
ZDB-ID	2020896-0
ISSN	1469-3178 ; 1469-221X
ISSN (online)	1469-3178
ISSN	1469-221X
DOI	10.15252/embr.201745497
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Zs.A 5433: 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)
Zs.MG 41: Show issues

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Article ; Online: Inhibition of Nuclear Pore Complex Formation Selectively Induces Cancer Cell Death.

Sakuma, Stephen / Raices, Marcela / Borlido, Joana / Guglielmi, Valeria / Zhu, Ethan Y S / D'Angelo, Maximiliano A

Cancer discovery

2020 Volume 11, Issue 1, Page(s) 176–193

Abstract: Nuclear pore complexes (NPC) are the central mediators of nucleocytoplasmic transport. Increasing evidence shows that many cancer cells have increased numbers of NPCs and become addicted to the nuclear transport machinery. How reducing NPC numbers ... ...

Abstract	Nuclear pore complexes (NPC) are the central mediators of nucleocytoplasmic transport. Increasing evidence shows that many cancer cells have increased numbers of NPCs and become addicted to the nuclear transport machinery. How reducing NPC numbers affects the physiology of normal and cancer cells and whether it could be exploited for cancer therapies has not been investigated. We report that inhibition of NPC formation, a process mostly restricted to proliferating cells, causes selective cancer cell death, prevents tumor growth, and induces tumor regression. Although cancer cells die in response to NPC assembly inhibition, normal cells undergo a reversible cell-cycle arrest that allows them to survive. Mechanistically, reducing NPC numbers results in multiple alterations contributing to cancer cell death, including abnormalities in nuclear transport, catastrophic alterations in gene expression, and the selective accumulation of DNA damage. Our findings uncover the NPC formation process as a novel targetable pathway in cancer cells. SIGNIFICANCE: Reducing NPC numbers in cancer cells induces death, prevents tumor growth, and results in tumor regression. Conversely, normal cells undergo a reversible cell-cycle arrest in response to inhibition of NPC assembly. These findings expose the potential of targeting NPC formation in cancer.
MeSH term(s)	Active Transport, Cell Nucleus ; Cell Death ; Humans ; Neoplasms/drug therapy ; Neoplasms/genetics ; Neoplasms/metabolism ; Nuclear Pore/metabolism ; Nuclear Pore Complex Proteins/metabolism
Chemical Substances	Nuclear Pore Complex Proteins
Language	English
Publishing date	2020-09-28
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Comment
ZDB-ID	2625242-9
ISSN	2159-8290 ; 2159-8274
ISSN (online)	2159-8290
ISSN	2159-8274
DOI	10.1158/2159-8290.CD-20-0581
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Zs.A 6916: Show issues

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Article ; Online: Identifying therapeutic targets for cancer among 2074 circulating proteins and risk of nine cancers.

Smith-Byrne, Karl / Hedman, Åsa / Dimitriou, Marios / Desai, Trishna / Sokolov, Alexandr V / Schioth, Helgi B / Koprulu, Mine / Pietzner, Maik / Langenberg, Claudia / Atkins, Joshua / Penha, Ricardo Cortez / McKay, James / Brennan, Paul / Zhou, Sirui / Richards, Brent J / Yarmolinsky, James / Martin, Richard M / Borlido, Joana / Mu, Xinmeng J /

Butterworth, Adam / Shen, Xia / Wilson, Jim / Assimes, Themistocles L / Hung, Rayjean J / Amos, Christopher / Purdue, Mark / Rothman, Nathaniel / Chanock, Stephen / Travis, Ruth C / Johansson, Mattias / Mälarstig, Anders

Nature communications

2024 Volume 15, Issue 1, Page(s) 3621

Abstract: Circulating proteins can reveal key pathways to cancer and identify therapeutic targets for cancer prevention. We investigate 2,074 circulating proteins and risk of nine common cancers (bladder, breast, endometrium, head and neck, lung, ovary, pancreas, ... ...

Abstract	Circulating proteins can reveal key pathways to cancer and identify therapeutic targets for cancer prevention. We investigate 2,074 circulating proteins and risk of nine common cancers (bladder, breast, endometrium, head and neck, lung, ovary, pancreas, kidney, and malignant non-melanoma) using cis protein Mendelian randomisation and colocalization. We conduct additional analyses to identify adverse side-effects of altering risk proteins and map cancer risk proteins to drug targets. Here we find 40 proteins associated with common cancers, such as PLAUR and risk of breast cancer [odds ratio per standard deviation increment: 2.27, 1.88-2.74], and with high-mortality cancers, such as CTRB1 and pancreatic cancer [0.79, 0.73-0.85]. We also identify potential adverse effects of protein-altering interventions to reduce cancer risk, such as hypertension. Additionally, we report 18 proteins associated with cancer risk that map to existing drugs and 15 that are not currently under clinical investigation. In sum, we identify protein-cancer links that improve our understanding of cancer aetiology. We also demonstrate that the wider consequence of any protein-altering intervention on well-being and morbidity is required to interpret any utility of proteins as potential future targets for therapeutic prevention.
MeSH term(s)	Humans ; Neoplasms/genetics ; Female ; Risk Factors ; Mendelian Randomization Analysis ; Biomarkers, Tumor/genetics ; Biomarkers, Tumor/metabolism ; Biomarkers, Tumor/blood ; Male ; Blood Proteins/metabolism
Chemical Substances	Biomarkers, Tumor ; Blood Proteins
Language	English
Publishing date	2024-04-29
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-024-46834-3
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Article ; Online: Nup62: a novel regulator of centrosome integrity and function.

Borlido, Joana / D'Angelo, Maximiliano A

Cell cycle (Georgetown, Tex.)

2013 Volume 13, Issue 1, Page(s) 14

MeSH term(s)	Animals ; Centrosome/physiology ; Humans ; Nuclear Pore Complex Proteins/metabolism
Chemical Substances	NUP62 protein, mouse ; Nuclear Pore Complex Proteins
Language	English
Publishing date	2013-11-22
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	2146183-1
ISSN	1551-4005 ; 1538-4101 ; 1554-8627
ISSN (online)	1551-4005
ISSN	1538-4101 ; 1554-8627
DOI	10.4161/cc.27299
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Zs.A 5881: Show issues

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Article ; Online: Nuclear pore complex-mediated modulation of TCR signaling is required for naïve CD4

Borlido, Joana / Sakuma, Stephen / Raices, Marcela / Carrette, Florent / Tinoco, Roberto / Bradley, Linda M / D'Angelo, Maximiliano A

Nature immunology

2018 Volume 19, Issue 6, Page(s) 594–605

Abstract: Nuclear pore complexes (NPCs) are channels connecting the nucleus with the cytoplasm. We report that loss of the tissue-specific NPC component Nup210 causes a severe deficit of naïve ... ...

Abstract	Nuclear pore complexes (NPCs) are channels connecting the nucleus with the cytoplasm. We report that loss of the tissue-specific NPC component Nup210 causes a severe deficit of naïve CD4
MeSH term(s)	Animals ; CD4-Positive T-Lymphocytes/immunology ; CD4-Positive T-Lymphocytes/metabolism ; Homeostasis/immunology ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Nuclear Pore/immunology ; Nuclear Pore/metabolism ; Nuclear Pore Complex Proteins/immunology ; Nuclear Pore Complex Proteins/metabolism ; Receptors, Antigen, T-Cell/immunology ; Receptors, Antigen, T-Cell/metabolism ; Signal Transduction/immunology
Chemical Substances	Nuclear Pore Complex Proteins ; Nup210 protein, mouse ; Receptors, Antigen, T-Cell
Language	English
Publishing date	2018-05-07
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2016987-5
ISSN	1529-2916 ; 1529-2908
ISSN (online)	1529-2916
ISSN	1529-2908
DOI	10.1038/s41590-018-0103-5
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Zs.A 5294: 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)
Zs.MG 42: Show issues

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Article ; Online: Nuclear Pores Regulate Muscle Development and Maintenance by Assembling a Localized Mef2C Complex.

Raices, Marcela / Bukata, Lucas / Sakuma, Stephen / Borlido, Joana / Hernandez, Leanora S / Hart, Daniel O / D'Angelo, Maximiliano A

Developmental cell

2017 Volume 41, Issue 5, Page(s) 540–554.e7

Abstract: Nuclear pore complexes (NPCs) are multiprotein channels connecting the nucleus with the cytoplasm. NPCs have been shown to have tissue-specific composition, suggesting that their function can be specialized. However, the physiological roles of NPC ... ...

Abstract	Nuclear pore complexes (NPCs) are multiprotein channels connecting the nucleus with the cytoplasm. NPCs have been shown to have tissue-specific composition, suggesting that their function can be specialized. However, the physiological roles of NPC composition changes and their impacts on cellular processes remain unclear. Here we show that the addition of the Nup210 nucleoporin to NPCs during myoblast differentiation results in assembly of an Mef2C transcriptional complex required for efficient expression of muscle structural genes and microRNAs. We show that this NPC-localized complex is essential for muscle growth, myofiber maturation, and muscle cell survival and that alterations in its activity result in muscle degeneration. Our findings suggest that NPCs regulate the activity of functional gene groups by acting as scaffolds that promote the local assembly of tissue-specific transcription complexes and show how nuclear pore composition changes can be exploited to regulate gene expression at the nuclear periphery.
MeSH term(s)	Animals ; Cell Differentiation ; Cell Nucleus/genetics ; Embryo, Nonmammalian/cytology ; Embryo, Nonmammalian/metabolism ; MEF2 Transcription Factors/genetics ; MEF2 Transcription Factors/metabolism ; Muscle Development/genetics ; Nuclear Envelope/genetics ; Nuclear Pore/physiology ; Nuclear Pore Complex Proteins/genetics ; Nuclear Pore Complex Proteins/metabolism ; Zebrafish/growth & development ; Zebrafish/metabolism ; Zebrafish Proteins/genetics ; Zebrafish Proteins/metabolism
Chemical Substances	MEF2 Transcription Factors ; Nuclear Pore Complex Proteins ; Zebrafish Proteins
Language	English
Publishing date	2017-06-05
Publishing country	United States
Document type	Journal Article
ZDB-ID	2054967-2
ISSN	1878-1551 ; 1534-5807
ISSN (online)	1878-1551
ISSN	1534-5807
DOI	10.1016/j.devcel.2017.05.007
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Zs.A 5742: 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)
Zs.MG 76: Show issues

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Article ; Online: Nuclear trafficking and functions of endocytic proteins implicated in oncogenesis.

Borlido, Joana / Zecchini, Vincent / Mills, Ian G

Traffic (Copenhagen, Denmark)

2009 Volume 10, Issue 9, Page(s) 1209–1220

Abstract: A subset of proteins predominantly associated with early endosomes or implicated in clathrin-mediated endocytosis can shuttle between the cytoplasm and the nucleus. Although the endocytic functions of these proteins have been extensively studied, much ... ...

Abstract	A subset of proteins predominantly associated with early endosomes or implicated in clathrin-mediated endocytosis can shuttle between the cytoplasm and the nucleus. Although the endocytic functions of these proteins have been extensively studied, much less effort has been expended in exploring their nuclear roles. Membrane trafficking proteins can affect signalling and proliferation and this can be achieved either at a nuclear or endocytic level. Furthermore, some proteins, such as Huntingtin interacting protein 1, are known as cancer biomarkers. This review will highlight the limits of our understanding of their nuclear functions and the relevance of this to signalling and oncogenesis.
MeSH term(s)	Active Transport, Cell Nucleus ; Adaptor Proteins, Vesicular Transport/genetics ; Adaptor Proteins, Vesicular Transport/metabolism ; Adaptor Proteins, Vesicular Transport/physiology ; Animals ; Cell Nucleus/metabolism ; Cytoplasm/metabolism ; Endocytosis ; Endosomes/metabolism ; Humans ; Neoplasms/genetics ; Neoplasms/metabolism
Chemical Substances	Adaptor Proteins, Vesicular Transport
Language	English
Publishing date	2009-05-12
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1483852-7
ISSN	1600-0854 ; 1398-9219
ISSN (online)	1600-0854
ISSN	1398-9219
DOI	10.1111/j.1600-0854.2009.00922.x
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Zs.A 5634: Show issues

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Article: Nuclear Trafficking and Functions of Endocytic Proteins Implicated in Oncogenesis

Borlido, Joana / Zecchini, Vincent / Mills, Ian G

Traffic. 2009 Sept., v. 10, no. 9

2009

Abstract	A subset of proteins predominantly associated with early endosomes or implicated in clathrin-mediated endocytosis can shuttle between the cytoplasm and the nucleus. Although the endocytic functions of these proteins have been extensively studied, much less effort has been expended in exploring their nuclear roles. Membrane trafficking proteins can affect signalling and proliferation and this can be achieved either at a nuclear or endocytic level. Furthermore, some proteins, such as Huntingtin interacting protein 1, are known as cancer biomarkers. This review will highlight the limits of our understanding of their nuclear functions and the relevance of this to signalling and oncogenesis.
Keywords	clathrin ; endocytosis
Language	English
Dates of publication	2009-09
Size	p. 1209-1220.
Publisher	Blackwell Publishing Ltd
Publishing place	Oxford, UK
Document type	Article
ZDB-ID	1483852-7
ISSN	1600-0854 ; 1398-9219
ISSN (online)	1600-0854
ISSN	1398-9219
DOI	10.1111/j.1600-0854.2009.00922.x
Database	NAL-Catalogue (AGRICOLA)

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Article: The Neuroprotective Action of Amidated-Kyotorphin on Amyloid β Peptide-Induced Alzheimer's Disease Pathophysiology.

Belo, Rita F / Martins, Margarida L F / Shvachiy, Liana / Costa-Coelho, Tiago / de Almeida-Borlido, Carolina / Fonseca-Gomes, João / Neves, Vera / Vicente Miranda, Hugo / Outeiro, Tiago F / Coelho, Joana E / Xapelli, Sara / Valente, Cláudia A / Heras, Montserrat / Bardaji, Eduard / Castanho, Miguel A R B / Diógenes, Maria José / Sebastião, Ana M

Frontiers in pharmacology

2020 Volume 11, Page(s) 985

Abstract: Kyotorphin (KTP, l-tyrosyl-l-arginine) is an endogenous dipeptide initially described to have analgesic properties. Recently, KTP was suggested to be an endogenous neuroprotective agent, namely for Alzheimer's disease (AD). In fact, KTP levels were shown ...

Abstract	Kyotorphin (KTP, l-tyrosyl-l-arginine) is an endogenous dipeptide initially described to have analgesic properties. Recently, KTP was suggested to be an endogenous neuroprotective agent, namely for Alzheimer's disease (AD). In fact, KTP levels were shown to be decreased in the cerebrospinal fluid of patients with AD, and recent data showed that intracerebroventricular (i.c.v.) injection of KTP ameliorates memory impairments in a sporadic rat model of AD. However, this administration route is far from being a suitable therapeutic strategy. Here, we evaluated if the blood-brain permeant KTP-derivative, KTP-NH
Language	English
Publishing date	2020-07-09
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2587355-6
ISSN	1663-9812
ISSN	1663-9812
DOI	10.3389/fphar.2020.00985
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Article ; Online: Clathrin is spindle-associated but not essential for mitosis.

Borlido, Joana / Veltri, Greg / Jackson, Antony P / Mills, Ian G

PloS one

2008 Volume 3, Issue 9, Page(s) e3115

Abstract: Background: Clathrin is a multimeric protein involved in vesicle coat assembly. Recently clathrin distribution was reported to change during the cell cycle and was found to associate with the mitotic spindle. Here we test whether the recruitment of ... ...

Abstract	Background: Clathrin is a multimeric protein involved in vesicle coat assembly. Recently clathrin distribution was reported to change during the cell cycle and was found to associate with the mitotic spindle. Here we test whether the recruitment of clathrin to the spindle is indicative of a critical functional contribution to mitosis. Methodology/principal findings: Previously a chicken pre-B lymphoma cell line (DKO-R) was developed in which the endogenous clathrin heavy chain alleles were replaced with the human clathrin heavy chain under the control of a tetracycline-regulatable promoter. Receptor-mediated and fluid-phase endocytosis were significantly inhibited in this line following clathrin knockout, and we used this to explore the significance of clathrin heavy chain expression for cell cycle progression. We confirmed using confocal microscopy that clathrin colocalised with tubulin at mitotic spindles. Using a propidium iodide flow cytometric assay we found no statistical difference in the cell cycle distribution of the knockout cells versus the wild-type. Additionally, we showed that the ploidy and the recovery kinetics following cell cycle arrest with nocodazole were unchanged by repressing clathrin heavy chain expression. Conclusions/significance: We conclude that the association of clathrin with the mitotic spindle and the contribution of clathrin to endocytosis are evolutionarily conserved. However we find that the contribution of clathrin to mitosis is less robust and dependent on cellular context. In other cell-lines silencing RNA has been used by others to knockdown clathrin expression resulting in an increase in the mitotic index of the cells. We show an effect on the G2/M phase population of clathrin knockdown in HEK293 cells but show that repressing clathrin expression in the DKO-R cell-line has no effect on the size of this population. Consequently this work highlights the need for a more detailed molecular understanding of the recruitment and function of clathrin at the spindle, since the localisation but not the impact of clathrin on mitosis appears to be robust in plants, mammalian and chicken B-cells.
MeSH term(s)	Alleles ; Animals ; Cell Cycle ; Cell Line ; Chickens ; Clathrin/metabolism ; Clathrin Heavy Chains/metabolism ; Cytoskeleton/metabolism ; Endocytosis ; Humans ; Microscopy, Confocal ; Mitosis ; Models, Biological ; Promoter Regions, Genetic ; Spindle Apparatus
Chemical Substances	Clathrin ; Clathrin Heavy Chains (114899-12-6)
Language	English
Publishing date	2008-09-03
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0003115
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