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Article ; Online: Endosomal microautophagy is an integrated part of the autophagic response to amino acid starvation.

Olsvik, Hallvard L / Svenning, Steingrim / Abudu, Yakubu Princely / Brech, Andreas / Stenmark, Harald / Johansen, Terje / Mejlvang, Jakob

Autophagy

2018 Volume 15, Issue 1, Page(s) 182–183

Abstract: Starvation is a fundamental type of stress naturally occurring in biological systems. All organisms have therefore evolved different safeguard mechanisms to cope with deficiencies in various types of nutrients. Cells, from yeast to humans, typically ... ...

Abstract	Starvation is a fundamental type of stress naturally occurring in biological systems. All organisms have therefore evolved different safeguard mechanisms to cope with deficiencies in various types of nutrients. Cells, from yeast to humans, typically respond to amino acid starvation by initiating degradation of cellular components by inducing autophagy. This degradation releases metabolic building blocks to sustain essential core cellular processes. Increasing evidence indicates that starvation-induced autophagy also acts to prepare cells for prolonged starvation by degrading key regulators of different cellular processes. In a recent study, we found that within the first hours of amino acid starvation cells elicit an autophagic response causing rapid degradation of specific proteins. The response is executed independently of both MTOR and canonical macroautophagy. Based on RNAi-mediated knockdown of essential components of the Endosomal Sorting Complex Required for Transport (ESCRT) machinery and electron microscopy we conclude that the response relies on some sort of endosomal microautophagy, hence vesicle budding into endosomes. Substantiated by the different substrates that are selectively degraded by this novel pathway we propose that the response predominantly acts to prepare cells for prolonged starvation. Intriguingly, this includes shutting down selective macroautophagy in preparation for a massive induction of bulk macroautophagy.
MeSH term(s)	Amino Acids ; Autophagy ; Endosomal Sorting Complexes Required for Transport ; Humans ; Microautophagy ; Starvation
Chemical Substances	Amino Acids ; Endosomal Sorting Complexes Required for Transport
Language	English
Publishing date	2018-10-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Comment
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2018.1532265
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Article ; Online: Starvation induces rapid degradation of selective autophagy receptors by endosomal microautophagy.

Mejlvang, Jakob / Olsvik, Hallvard / Svenning, Steingrim / Bruun, Jack-Ansgar / Abudu, Yakubu Princely / Larsen, Kenneth Bowitz / Brech, Andreas / Hansen, Tom E / Brenne, Hanne / Hansen, Terkel / Stenmark, Harald / Johansen, Terje

The Journal of cell biology

2018 Volume 217, Issue 10, Page(s) 3640–3655

Abstract: It is not clear to what extent starvation-induced autophagy affects the proteome on a global scale and whether it is selective. In this study, we report based on quantitative proteomics that cells during the first 4 h of acute starvation elicit lysosomal ...

Abstract	It is not clear to what extent starvation-induced autophagy affects the proteome on a global scale and whether it is selective. In this study, we report based on quantitative proteomics that cells during the first 4 h of acute starvation elicit lysosomal degradation of up to 2-3% of the proteome. The most significant changes are caused by an immediate autophagic response elicited by shortage of amino acids but executed independently of mechanistic target of rapamycin and macroautophagy. Intriguingly, the autophagy receptors p62/SQSTM1, NBR1, TAX1BP1, NDP52, and NCOA4 are among the most efficiently degraded substrates. Already 1 h after induction of starvation, they are rapidly degraded by a process that selectively delivers autophagy receptors to vesicles inside late endosomes/multivesicular bodies depending on the endosomal sorting complex required for transport III (ESCRT-III). Our data support a model in which amino acid deprivation elicits endocytosis of specific membrane receptors, induction of macroautophagy, and rapid degradation of autophagy receptors by endosomal microautophagy.
MeSH term(s)	Autophagy ; Endosomal Sorting Complexes Required for Transport/genetics ; Endosomal Sorting Complexes Required for Transport/metabolism ; Endosomes/genetics ; Endosomes/metabolism ; HeLa Cells ; Humans ; Intracellular Signaling Peptides and Proteins/genetics ; Intracellular Signaling Peptides and Proteins/metabolism ; Models, Biological ; Neoplasm Proteins/genetics ; Neoplasm Proteins/metabolism ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Nuclear Receptor Coactivators/genetics ; Proteins/genetics ; Proteins/metabolism ; RNA-Binding Proteins/genetics ; Sequestosome-1 Protein/genetics ; Sequestosome-1 Protein/metabolism
Chemical Substances	CALCOCO2 protein, human ; Endosomal Sorting Complexes Required for Transport ; Intracellular Signaling Peptides and Proteins ; NBR1 protein, human ; NCOA4 protein, human ; Neoplasm Proteins ; Nuclear Proteins ; Nuclear Receptor Coactivators ; P62 protein, human ; Proteins ; RNA-Binding Proteins ; SQSTM1 protein, human ; Sequestosome-1 Protein ; TAX1BP1 protein, human
Language	English
Publishing date	2018-07-17
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.201711002
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Article ; Online: Tousled-like kinases phosphorylate Asf1 to promote histone supply during DNA replication.

Klimovskaia, Ilnaz M / Young, Clifford / Strømme, Caroline B / Menard, Patrice / Jasencakova, Zuzana / Mejlvang, Jakob / Ask, Katrine / Ploug, Michael / Nielsen, Michael L / Jensen, Ole N / Groth, Anja

Nature communications

2014 Volume 5, Page(s) 3394

Abstract: During DNA replication, nucleosomes are rapidly assembled on newly synthesized DNA to restore chromatin organization. Asf1, a key histone H3-H4 chaperone required for this process, is phosphorylated by Tousled-like kinases (TLKs). Here, we identify TLK ... ...

Abstract	During DNA replication, nucleosomes are rapidly assembled on newly synthesized DNA to restore chromatin organization. Asf1, a key histone H3-H4 chaperone required for this process, is phosphorylated by Tousled-like kinases (TLKs). Here, we identify TLK phosphorylation sites by mass spectrometry and dissect how phosphorylation has an impact on human Asf1 function. The divergent C-terminal tail of Asf1a is phosphorylated at several sites, and this is required for timely progression through S phase. Consistent with this, biochemical analysis of wild-type and phospho-mimetic Asf1a shows that phosphorylation enhances binding to histones and the downstream chaperones CAF-1 and HIRA. Moreover, we find that TLK phosphorylation of Asf1a is induced in cells experiencing deficiency of new histones and that TLK interaction with Asf1a involves its histone-binding pocket. We thus propose that TLK signalling promotes histone supply in S phase by targeting histone-free Asf1 and stimulating its ability to shuttle histones to sites of chromatin assembly.
MeSH term(s)	Amino Acid Sequence ; Binding Sites/genetics ; Blotting, Western ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Cell Line, Tumor ; Chromatin/genetics ; Chromatin/metabolism ; DNA Replication ; HeLa Cells ; Histones/metabolism ; Humans ; Mass Spectrometry ; Microscopy, Confocal ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Mutation ; Phosphorylation ; Protein Binding ; Protein Serine-Threonine Kinases/genetics ; Protein Serine-Threonine Kinases/metabolism ; RNA Interference ; S Phase/genetics
Chemical Substances	ASF1A protein, human ; ASF1B protein, human ; Cell Cycle Proteins ; Chromatin ; Histones ; Molecular Chaperones ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; TLK1 protein, human (EC 2.7.11.1)
Language	English
Publishing date	2014-03-06
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/ncomms4394
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Article ; Online: Nascent chromatin capture proteomics determines chromatin dynamics during DNA replication and identifies unknown fork components.

Alabert, Constance / Bukowski-Wills, Jimi-Carlo / Lee, Sung-Bau / Kustatscher, Georg / Nakamura, Kyosuke / de Lima Alves, Flavia / Menard, Patrice / Mejlvang, Jakob / Rappsilber, Juri / Groth, Anja

Nature cell biology

2014 Volume 16, Issue 3, Page(s) 281–293

Abstract: To maintain genome function and stability, DNA sequence and its organization into chromatin must be duplicated during cell division. Understanding how entire chromosomes are copied remains a major challenge. Here, we use nascent chromatin capture (NCC) ... ...

Abstract	To maintain genome function and stability, DNA sequence and its organization into chromatin must be duplicated during cell division. Understanding how entire chromosomes are copied remains a major challenge. Here, we use nascent chromatin capture (NCC) to profile chromatin proteome dynamics during replication in human cells. NCC relies on biotin-dUTP labelling of replicating DNA, affinity purification and quantitative proteomics. Comparing nascent chromatin with mature post-replicative chromatin, we provide association dynamics for 3,995 proteins. The replication machinery and 485 chromatin factors such as CAF-1, DNMT1 and SUV39h1 are enriched in nascent chromatin, whereas 170 factors including histone H1, DNMT3, MBD1-3 and PRC1 show delayed association. This correlates with H4K5K12diAc removal and H3K9me1 accumulation, whereas H3K27me3 and H3K9me3 remain unchanged. Finally, we combine NCC enrichment with experimentally derived chromatin probabilities to predict a function in nascent chromatin for 93 uncharacterized proteins, and identify FAM111A as a replication factor required for PCNA loading. Together, this provides an extensive resource to understand genome and epigenome maintenance.
MeSH term(s)	Chromatin/metabolism ; Chromatin Assembly and Disassembly ; Chromosomal Proteins, Non-Histone/isolation & purification ; Chromosomal Proteins, Non-Histone/metabolism ; DNA Replication ; DNA-Binding Proteins/isolation & purification ; DNA-Binding Proteins/metabolism ; HeLa Cells ; Histones/isolation & purification ; Histones/metabolism ; Humans ; Proliferating Cell Nuclear Antigen/metabolism ; Protein Transport ; Proteome/isolation & purification ; Proteome/metabolism ; Proteomics ; Receptors, Virus/metabolism ; S Phase Cell Cycle Checkpoints
Chemical Substances	Chromatin ; Chromosomal Proteins, Non-Histone ; DNA-Binding Proteins ; FAM111A protein, human ; Histones ; Proliferating Cell Nuclear Antigen ; Proteome ; Receptors, Virus
Language	English
Publishing date	2014-02-23
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1474722-4
ISSN	1476-4679 ; 1465-7392
ISSN (online)	1476-4679
ISSN	1465-7392
DOI	10.1038/ncb2918
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Zs.A 5169: 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 12: Show issues

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Article ; Online: New histone supply regulates replication fork speed and PCNA unloading.

Mejlvang, Jakob / Feng, Yunpeng / Alabert, Constance / Neelsen, Kai J / Jasencakova, Zuzana / Zhao, Xiaobei / Lees, Michael / Sandelin, Albin / Pasero, Philippe / Lopes, Massimo / Groth, Anja

The Journal of cell biology

2013 Volume 204, Issue 1, Page(s) 29–43

Abstract: Correct duplication of DNA sequence and its organization into chromatin is central to genome function and stability. However, it remains unclear how cells coordinate DNA synthesis with provision of new histones for chromatin assembly to ensure ... ...

Abstract	Correct duplication of DNA sequence and its organization into chromatin is central to genome function and stability. However, it remains unclear how cells coordinate DNA synthesis with provision of new histones for chromatin assembly to ensure chromosomal stability. In this paper, we show that replication fork speed is dependent on new histone supply and efficient nucleosome assembly. Inhibition of canonical histone biosynthesis impaired replication fork progression and reduced nucleosome occupancy on newly synthesized DNA. Replication forks initially remained stable without activation of conventional checkpoints, although prolonged histone deficiency generated DNA damage. PCNA accumulated on newly synthesized DNA in cells lacking new histones, possibly to maintain opportunity for CAF-1 recruitment and nucleosome assembly. Consistent with this, in vitro and in vivo analysis showed that PCNA unloading is delayed in the absence of nucleosome assembly. We propose that coupling of fork speed and PCNA unloading to nucleosome assembly provides a simple mechanism to adjust DNA replication and maintain chromatin integrity during transient histone shortage.
MeSH term(s)	Cell Line, Tumor ; Chromatin/genetics ; Chromatin/metabolism ; Chromatin Assembly Factor-1/genetics ; Chromatin Assembly Factor-1/metabolism ; Chromatin Assembly and Disassembly/genetics ; DNA Damage/genetics ; DNA Replication ; HeLa Cells ; Histones/genetics ; Histones/metabolism ; Humans ; Nucleosomes/genetics ; Nucleosomes/metabolism ; Proliferating Cell Nuclear Antigen/genetics ; Proliferating Cell Nuclear Antigen/metabolism ; RNA, Messenger/genetics ; Transcription Factors
Chemical Substances	CNOT8 protein, human ; Chromatin ; Chromatin Assembly Factor-1 ; Histones ; Nucleosomes ; Proliferating Cell Nuclear Antigen ; RNA, Messenger ; Transcription Factors
Language	English
Publishing date	2013-12-30
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.201305017
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Article ; Online: Cyclin-dependent kinase suppression by WEE1 kinase protects the genome through control of replication initiation and nucleotide consumption.

Beck, Halfdan / Nähse-Kumpf, Viola / Larsen, Marie Sofie Yoo / O'Hanlon, Karen A / Patzke, Sebastian / Holmberg, Christian / Mejlvang, Jakob / Groth, Anja / Nielsen, Olaf / Syljuåsen, Randi G / Sørensen, Claus Storgaard

Molecular and cellular biology

2012 Volume 32, Issue 20, Page(s) 4226–4236

Abstract: Activation of oncogenes or inhibition of WEE1 kinase deregulates cyclin-dependent kinase (CDK) activity and leads to replication stress; however, the underlying mechanism is not understood. We now show that elevation of CDK activity by inhibition of WEE1 ...

Abstract	Activation of oncogenes or inhibition of WEE1 kinase deregulates cyclin-dependent kinase (CDK) activity and leads to replication stress; however, the underlying mechanism is not understood. We now show that elevation of CDK activity by inhibition of WEE1 kinase rapidly increases initiation of replication. This leads to nucleotide shortage and reduces replication fork speed, which is followed by SLX4/MUS81-mediated DNA double-strand breakage. Fork speed is normalized and DNA double-strand break (DSB) formation is suppressed when CDT1, a key factor for replication initiation, is depleted. Furthermore, addition of nucleosides counteracts the effects of unscheduled CDK activity on fork speed and DNA DSB formation. Finally, we show that WEE1 regulates the ionizing radiation (IR)-induced S-phase checkpoint, consistent with its role in control of replication initiation. In conclusion, these results suggest that deregulated CDK activity, such as that occurring following inhibition of WEE1 kinase or activation of oncogenes, induces replication stress and loss of genomic integrity through increased firing of replication origins and subsequent nucleotide shortage.
MeSH term(s)	CDC2 Protein Kinase/antagonists & inhibitors ; CDC2 Protein Kinase/metabolism ; Cell Cycle Proteins/metabolism ; Cell Line ; DNA Breaks, Double-Stranded ; DNA Replication ; Genome, Human ; Genomic Instability ; Humans ; Nuclear Proteins/metabolism ; Nucleotides/metabolism ; Protein-Tyrosine Kinases/metabolism ; Recombinases/metabolism ; S Phase Cell Cycle Checkpoints/radiation effects
Chemical Substances	CDT1 protein, human ; Cell Cycle Proteins ; Nuclear Proteins ; Nucleotides ; Recombinases ; Protein-Tyrosine Kinases (EC 2.7.10.1) ; WEE1 protein, human (EC 2.7.10.2) ; CDC2 Protein Kinase (EC 2.7.11.22) ; SLX4 protein, human (EC 3.1.-)
Language	English
Publishing date	2012-08-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1128/MCB.00412-12
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Zs.A 1666: Show issues

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Article ; Online: Cyclin-Dependent Kinase Suppression by WEE1 Kinase Protects the Genome through Control of Replication Initiation and Nucleotide Consumption

Beck, Halfdan / Nähse-Kumpf, Viola / Larsen, Marie Sofie Yoo / O'Hanlon, Karen A. / Patzke, Sebastian / Holmberg, Christian / Mejlvang, Jakob / Groth, Anja / Nielsen, Olaf / Syljuåsen, Randi G. / Sørensen, Claus Storgaard

Molecular and Cellular Biology. 2012 Oct. 1, v. 32, no. 20 p.4226-4236

2012

Abstract	Activation of oncogenes or inhibition of WEE1 kinase deregulates cyclin-dependent kinase (CDK) activity and leads to replication stress; however, the underlying mechanism is not understood. We now show that elevation of CDK activity by inhibition of WEE1 kinase rapidly increases initiation of replication. This leads to nucleotide shortage and reduces replication fork speed, which is followed by SLX4/MUS81-mediated DNA double-strand breakage. Fork speed is normalized and DNA double-strand break (DSB) formation is suppressed when CDT1, a key factor for replication initiation, is depleted. Furthermore, addition of nucleosides counteracts the effects of unscheduled CDK activity on fork speed and DNA DSB formation. Finally, we show that WEE1 regulates the ionizing radiation (IR)-induced S-phase checkpoint, consistent with its role in control of replication initiation. In conclusion, these results suggest that deregulated CDK activity, such as that occurring following inhibition of WEE1 kinase or activation of oncogenes, induces replication stress and loss of genomic integrity through increased firing of replication origins and subsequent nucleotide shortage.
Keywords	DNA ; DNA damage ; cell biology ; cyclin-dependent kinase ; genomics ; nucleosides ; oncogenes
Language	English
Dates of publication	2012-1001
Size	p. 4226-4236.
Publishing place	Taylor & Francis
Document type	Article ; Online
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1128/MCB.00412-12
Database	NAL-Catalogue (AGRICOLA)

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Article: Direct repression of cyclin D1 by SIP1 attenuates cell cycle progression in cells undergoing an epithelial mesenchymal transition.

Mejlvang, Jakob / Kriajevska, Marina / Vandewalle, Cindy / Chernova, Tatyana / Sayan, A Emre / Berx, Geert / Mellon, J Kilian / Tulchinsky, Eugene

Molecular biology of the cell

2007 Volume 18, Issue 11, Page(s) 4615–4624

Abstract: Zinc finger transcription factors of the Snail/Slug and ZEB-1/SIP1 families control epithelial-mesenchymal transitions in development in cancer. Here, we studied SIP1-regulated mesenchymal conversion of epidermoid A431 cells. We found that concomitant ... ...

Abstract	Zinc finger transcription factors of the Snail/Slug and ZEB-1/SIP1 families control epithelial-mesenchymal transitions in development in cancer. Here, we studied SIP1-regulated mesenchymal conversion of epidermoid A431 cells. We found that concomitant with inducing invasive phenotype, SIP1 inhibited expression of cyclin D1 and induced hypophosphorylation of the Rb tumor suppressor protein. Repression of cyclin D1 was caused by direct binding of SIP1 to three sequence elements in the cyclin D1 gene promoter. By expressing exogenous cyclin D1 in A431/SIP1 cells and using RNA interference, we demonstrated that the repression of cyclin D1 gene by SIP1 was necessary and sufficient for Rb hypophosphorylation and accumulation of cells in G1 phase. A431 cells expressing SIP1 along with exogenous cyclin D1 were highly invasive, indicating that SIP1-regulated invasion is independent of attenuation of G1/S progression. However, in another epithelial-mesenchymal transition model, gradual mesenchymal conversion of A431 cells induced by a dominant negative mutant of E-cadherin produced no effect on the cell cycle. We suggest that impaired G1/S phase progression is a general feature of cells that have undergone EMT induced by transcription factors of the Snail/Slug and ZEB-1/SIP1 families.
MeSH term(s)	Cadherins/genetics ; Cadherins/metabolism ; Cell Cycle ; Cell Line, Tumor ; Cyclin D1/genetics ; Cyclin D1/metabolism ; Down-Regulation ; Epithelial Cells/cytology ; Epithelial Cells/metabolism ; Humans ; Mesoderm/cytology ; Mesoderm/metabolism ; Mutation/genetics ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Promoter Regions, Genetic/genetics ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; Transcription, Genetic/genetics
Chemical Substances	Cadherins ; GEMIN2 protein, human ; Nerve Tissue Proteins ; RNA-Binding Proteins ; Cyclin D1 (136601-57-5)
Language	English
Publishing date	2007-09-12
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.e07-05-0406
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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: Characterization of E-cadherin-dependent and -independent events in a new model of c-Fos-mediated epithelial-mesenchymal transition.

Mejlvang, Jakob / Kriajevska, Marina / Berditchevski, Fedor / Bronstein, Igor / Lukanidin, Eugene M / Pringle, J Howard / Mellon, J Kilian / Tulchinsky, Eugene M

Experimental cell research

2007 Volume 313, Issue 2, Page(s) 380–393

Abstract: Fos proteins have been implicated in control of tumorigenesis-related genetic programs including invasion, angiogenesis, cell proliferation and apoptosis. In this study, we demonstrate that c-Fos is able to induce mesenchymal transition in murine ... ...

Abstract	Fos proteins have been implicated in control of tumorigenesis-related genetic programs including invasion, angiogenesis, cell proliferation and apoptosis. In this study, we demonstrate that c-Fos is able to induce mesenchymal transition in murine tumorigenic epithelial cell lines. Expression of c-Fos in MT1TC1 cells led to prominent alterations in cell morphology, increased expression of mesenchymal markers, vimentin and S100A4, DNA methylation-dependent down-regulation of E-cadherin and abrogation of cell-cell adhesion. In addition, c-Fos induced a strong beta-catenin-independent proliferative response in MT1TC1 cells and stimulated cell motility, invasion and adhesion to different extracellular matrix proteins. To explore whether loss of E-cadherin plays a role in c-Fos-mediated mesenchymal transition, we expressed wild-type E-cadherin and two different E-cadherin mutants in MT1TC1/c-fos cells. Expression of wild-type E-cadherin restored epithelioid morphology and enhanced cellular levels of catenins. However, exogenous E-cadherin did not influence expression of c-Fos-dependent genes, only partly suppressed growth of MT1TC1/c-fos cells and produced no effect on c-Fos-stimulated cell motility and invasion in matrigel. On the other hand, re-expression of E-cadherin specifically negated c-Fos-induced adhesion to collagen type I, but not to laminin or fibronectin. Of interest, mutant E-cadherin which lacks the ability to form functional adhesive complexes had an opposite, potentiating effect on cell adhesion to collagen I. These data suggest that cell adhesion to collagen I is regulated by the functional state of E-cadherin. Overall, our data demonstrate that, with the exception of adhesion to collagen I, c-Fos is dominant over E-cadherin in relation to the aspects of mesenchymal transition assayed in this study.
MeSH term(s)	Adenocarcinoma/genetics ; Adenocarcinoma/pathology ; Animals ; Cadherins/genetics ; Cell Adhesion/genetics ; Cell Line, Tumor ; Cell Movement/genetics ; Cell Proliferation ; DNA Methylation ; Epigenesis, Genetic ; Epithelial Cells/pathology ; Extracellular Matrix/metabolism ; Gene Expression Regulation, Neoplastic ; Mesoderm/pathology ; Mice ; Models, Biological ; Mutation ; Neoplasm Invasiveness/genetics ; Neoplasm Invasiveness/pathology ; Promoter Regions, Genetic ; Proto-Oncogene Proteins c-fos/physiology ; beta Catenin/metabolism
Chemical Substances	Cadherins ; Proto-Oncogene Proteins c-fos ; beta Catenin
Language	English
Publishing date	2007-01-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1493-x
ISSN	1090-2422 ; 0014-4827
ISSN (online)	1090-2422
ISSN	0014-4827
DOI	10.1016/j.yexcr.2006.10.017
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Zs.A 563: Show issues

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Article: Immediate and delayed effects of E-cadherin inhibition on gene regulation and cell motility in human epidermoid carcinoma cells.

Andersen, Henriette / Mejlvang, Jakob / Mahmood, Shaukat / Gromova, Irina / Gromov, Pavel / Lukanidin, Eugene / Kriajevska, Marina / Mellon, J Kilian / Tulchinsky, Eugene

Molecular and cellular biology

2005 Volume 25, Issue 20, Page(s) 9138–9150

Abstract: The invasion suppressor protein, E-cadherin, plays a central role in epithelial cell-cell adhesion. Loss of E-cadherin expression or function in various tumors of epithelial origin is associated with a more invasive phenotype. In this study, by ... ...

Abstract	The invasion suppressor protein, E-cadherin, plays a central role in epithelial cell-cell adhesion. Loss of E-cadherin expression or function in various tumors of epithelial origin is associated with a more invasive phenotype. In this study, by expressing a dominant-negative mutant of E-cadherin (Ec1WVM) in A431 cells, we demonstrated that specific inhibition of E-cadherin-dependent cell-cell adhesion led to the genetic reprogramming of tumor cells. In particular, prolonged inhibition of cell-cell adhesion activated expression of vimentin and repressed cytokeratins, suggesting that the effects of Ec1WVM can be classified as epithelial-mesenchymal transition. Both short-term and prolonged expression of Ec1WVM resulted in morphological transformation and increased cell migration though to different extents. Short-term expression of Ec1WVM up-regulated two AP-1 family members, c-jun and fra-1, but was insufficient to induce complete mesenchymal transition. AP-1 activity induced by the short-term expression of Ec1WVM was required for transcriptional up-regulation of AP-1 family members and down-regulation of two other Ec1WVM-responsive genes, S100A4 and igfbp-3. Using a dominant-negative mutant of c-Jun (TAM67) and RNA interference-mediated silencing of c-Jun and Fra-1, we demonstrated that AP-1 was required for cell motility stimulated by the expression of Ec1WVM. In contrast, Ec1WVM-mediated changes in cell morphology were AP-1-independent. Our data suggest that mesenchymal transition induced by prolonged functional inhibition of E-cadherin is a slow and gradual process. At the initial step of this process, Ec1WVM triggers a positive autoregulatory mechanism that increases AP-1 activity. Activated AP-1 in turn contributes to Ec1WVM-mediated effects on gene expression and tumor cell motility. These data provide novel insight into the tumor suppressor function of E-cadherin.
MeSH term(s)	Base Sequence ; Cadherins/genetics ; Cadherins/physiology ; Carcinoma, Squamous Cell/genetics ; Carcinoma, Squamous Cell/pathology ; Carcinoma, Squamous Cell/physiopathology ; Cell Adhesion/genetics ; Cell Adhesion/physiology ; Cell Line, Tumor ; Cell Movement/genetics ; Cell Movement/physiology ; DNA, Neoplasm/genetics ; Gene Expression Regulation, Neoplastic ; Humans ; Kinetics ; Mutation ; Phosphorylation ; RNA Interference ; Receptor, Epidermal Growth Factor/metabolism ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Transcription Factor AP-1/metabolism ; Transfection
Chemical Substances	Cadherins ; DNA, Neoplasm ; Recombinant Proteins ; Transcription Factor AP-1 ; Receptor, Epidermal Growth Factor (EC 2.7.10.1)
Language	English
Publishing date	2005-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1128/MCB.25.20.9138-9150.2005
Database	MEDical Literature Analysis and Retrieval System OnLINE

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