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Article ; Online: Celsr1 adhesive interactions mediate the asymmetric organization of planar polarity complexes.

Stahley, Sara N / Basta, Lena P / Sharan, Rishabh / Devenport, Danelle

2021 Volume 10

Abstract: To orchestrate collective polarization across tissues, planar cell polarity (PCP) proteins localize asymmetrically to cell junctions, a conserved feature of PCP that requires the atypical cadherin Celsr1. We report that mouse Celsr1 engages in ... ...

Abstract	To orchestrate collective polarization across tissues, planar cell polarity (PCP) proteins localize asymmetrically to cell junctions, a conserved feature of PCP that requires the atypical cadherin Celsr1. We report that mouse Celsr1 engages in both
MeSH term(s)	Animals ; Cell Line ; Cell Polarity/physiology ; Embryo, Mammalian/metabolism ; Embryo, Mammalian/physiology ; Female ; Frizzled Receptors/metabolism ; Humans ; Keratinocytes/metabolism ; Keratinocytes/ultrastructure ; Male ; Mice ; Receptors, G-Protein-Coupled/metabolism
Chemical Substances	Celsr1 protein, mouse ; Frizzled Receptors ; Receptors, G-Protein-Coupled
Language	English
Publishing date	2021-02-02
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.62097
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Article ; Online: Celsr1 adhesive interactions mediate the asymmetric organization of planar polarity complexes

Sara N Stahley / Lena P Basta / Rishabh Sharan / Danelle Devenport

eLife, Vol

2021 Volume 10

Abstract	To orchestrate collective polarization across tissues, planar cell polarity (PCP) proteins localize asymmetrically to cell junctions, a conserved feature of PCP that requires the atypical cadherin Celsr1. We report that mouse Celsr1 engages in both trans- and cis-interactions, and organizes into dense and highly stable punctate assemblies. We provide evidence suggesting that PCP-mutant variant of Celsr1, Celsr1Crsh, selectively impairs lateral cis-interactions. Although Celsr1Crsh mediates cell adhesion in trans, it displays increased mobility, diminishes junctional enrichment, and fails to engage in homophilic adhesion with the wild-type protein, phenotypes that can be rescued by ectopic cis-dimerization. Using biochemical and super-resolution microscopy approaches, we show that although Celsr1Crsh physically interacts with PCP proteins Frizzled6 and Vangl2, it fails to organize these proteins into asymmetric junctional complexes. Our results suggest mammalian Celsr1 functions not only as a trans-adhesive homodimeric bridge, but also as an organizer of intercellular Frizzled6 and Vangl2 asymmetry through lateral, cis-interactions.
Keywords	planar cell polarity ; super resolution microscopy ; epithelia ; epidermis ; cadherin ; cell junctions ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
Subject code	571
Language	English
Publishing date	2021-02-01T00:00:00Z
Publisher	eLife Sciences Publications Ltd
Document type	Article ; Online
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Article ; Online: Desmosomes in acquired disease.

Stahley, Sara N / Kowalczyk, Andrew P

Cell and tissue research

2015 Volume 360, Issue 3, Page(s) 439–456

Abstract: Desmosomes are cell-cell junctions that mediate adhesion and couple the intermediate filament cytoskeleton to sites of cell-cell contact. This architectural arrangement integrates adhesion and cytoskeletal elements of adjacent cells. The importance of ... ...

Abstract	Desmosomes are cell-cell junctions that mediate adhesion and couple the intermediate filament cytoskeleton to sites of cell-cell contact. This architectural arrangement integrates adhesion and cytoskeletal elements of adjacent cells. The importance of this robust adhesion system is evident in numerous human diseases, both inherited and acquired, which occur when desmosome function is compromised. This review focuses on autoimmune and infectious diseases that impair desmosome function. In addition, we discuss emerging evidence that desmosomal genes are often misregulated in cancer. The emphasis of our discussion is placed on the way in which human diseases can inform our understanding of basic desmosome biology and in turn, the means by which fundamental advances in the cell biology of desmosomes might lead to new treatments for acquired diseases of the desmosome.
MeSH term(s)	Animals ; Desmosomes/metabolism ; Humans ; Models, Biological ; Skin Diseases/metabolism ; Skin Diseases/pathology
Language	English
Publishing date	2015-03-21
Publishing country	Germany
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	125067-x
ISSN	1432-0878 ; 0302-766X
ISSN (online)	1432-0878
ISSN	0302-766X
DOI	10.1007/s00441-015-2155-2
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Article ; Online: Author Correction: Architecture and dynamics of a desmosome-endoplasmic reticulum complex.

Bharathan, Navaneetha Krishnan / Giang, William / Hoffman, Coryn L / Aaron, Jesse S / Khuon, Satya / Chew, Teng-Leong / Preibisch, Stephan / Trautman, Eric T / Heinrich, Larissa / Bogovic, John / Bennett, Davis / Ackerman, David / Park, Woohyun / Petruncio, Alyson / Weigel, Aubrey V / Saalfeld, Stephan / Wayne Vogl, A / Stahley, Sara N / Kowalczyk, Andrew P

Nature cell biology

2024 Volume 26, Issue 4, Page(s) 660

Language	English
Publishing date	2024-02-13
Publishing country	England
Document type	Published Erratum
ZDB-ID	1474722-4
ISSN	1476-4679 ; 1465-7392
ISSN (online)	1476-4679
ISSN	1465-7392
DOI	10.1038/s41556-024-01376-0
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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)
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Article ; Online: Architecture and dynamics of a desmosome-endoplasmic reticulum complex.

Nature cell biology

2023 Volume 25, Issue 6, Page(s) 823–835

Abstract: The endoplasmic reticulum (ER) forms a dynamic network that contacts other cellular membranes to regulate stress responses, calcium signalling and lipid transfer. Here, using high-resolution volume electron microscopy, we find that the ER forms a ... ...

Abstract	The endoplasmic reticulum (ER) forms a dynamic network that contacts other cellular membranes to regulate stress responses, calcium signalling and lipid transfer. Here, using high-resolution volume electron microscopy, we find that the ER forms a previously unknown association with keratin intermediate filaments and desmosomal cell-cell junctions. Peripheral ER assembles into mirror image-like arrangements at desmosomes and exhibits nanometre proximity to keratin filaments and the desmosome cytoplasmic plaque. ER tubules exhibit stable associations with desmosomes, and perturbation of desmosomes or keratin filaments alters ER organization, mobility and expression of ER stress transcripts. These findings indicate that desmosomes and the keratin cytoskeleton regulate the distribution, function and dynamics of the ER network. Overall, this study reveals a previously unknown subcellular architecture defined by the structural integration of ER tubules with an epithelial intercellular junction.
MeSH term(s)	Desmosomes/chemistry ; Desmosomes/metabolism ; Desmosomes/ultrastructure ; Cytoskeleton/metabolism ; Keratins/metabolism ; Intermediate Filaments/metabolism ; Intermediate Filaments/ultrastructure ; Endoplasmic Reticulum/metabolism
Chemical Substances	Keratins (68238-35-7)
Language	English
Publishing date	2023-06-08
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	1474722-4
ISSN	1476-4679 ; 1465-7392
ISSN (online)	1476-4679
ISSN	1465-7392
DOI	10.1038/s41556-023-01154-4
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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)
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Article ; Online: Plakophilin-1 protects keratinocytes from pemphigus vulgaris IgG by forming calcium-independent desmosomes.

Tucker, Dana K / Stahley, Sara N / Kowalczyk, Andrew P

The Journal of investigative dermatology

2013 Volume 134, Issue 4, Page(s) 1033–1043

Abstract: Plakophilin-1 (PKP-1) is an armadillo family protein critical for desmosomal adhesion and epidermal integrity. In the autoimmune skin-blistering disease pemphigus vulgaris (PV), autoantibodies (IgG) target the desmosomal cadherin desmoglein 3 (Dsg3) and ... ...

Abstract	Plakophilin-1 (PKP-1) is an armadillo family protein critical for desmosomal adhesion and epidermal integrity. In the autoimmune skin-blistering disease pemphigus vulgaris (PV), autoantibodies (IgG) target the desmosomal cadherin desmoglein 3 (Dsg3) and compromise keratinocyte cell-cell adhesion. Here, we report that enhanced expression of PKP-1 protects keratinocytes from PV IgG-induced loss of cell-cell adhesion. PKP-1 prevents loss of Dsg3 and other desmosomal proteins from cell-cell borders and prevents alterations in desmosome ultrastructure in keratinocytes treated with PV IgG. Using a series of Dsg3 chimeras and deletion constructs, we find that PKP-1 clusters Dsg3 with the desmosomal plaque protein desmoplakin in a manner dependent on the plakoglobin-binding domain of the Dsg3 tail. Furthermore, PKP-1 expression transforms desmosome adhesion from a calcium-dependent to a calcium-independent and hyperadhesive state. These results demonstrate that manipulating the expression of a single desmosomal plaque protein can block the pathogenic effects of PV IgG on keratinocyte adhesion.
MeSH term(s)	Calcium/chemistry ; Cell Adhesion ; Cells, Cultured ; Chelating Agents/chemistry ; Desmoglein 3/chemistry ; Desmosomes/metabolism ; Detergents/chemistry ; Endocytosis ; Epidermis/metabolism ; Gene Expression Regulation ; Humans ; Immunoglobulin G/chemistry ; Keratinocytes/cytology ; Pemphigus/immunology ; Pemphigus/metabolism ; Plakophilins/metabolism
Chemical Substances	Chelating Agents ; Desmoglein 3 ; Detergents ; Immunoglobulin G ; PKP1 protein, human ; Plakophilins ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2013-09-20
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	80136-7
ISSN	1523-1747 ; 0022-202X
ISSN (online)	1523-1747
ISSN	0022-202X
DOI	10.1038/jid.2013.401
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Article ; Online: E-cadherin binds to desmoglein to facilitate desmosome assembly.

Shafraz, Omer / Rübsam, Matthias / Stahley, Sara N / Caldara, Amber L / Kowalczyk, Andrew P / Niessen, Carien M / Sivasankar, Sanjeevi

eLife

2018 Volume 7

Abstract: Desmosomes are adhesive junctions composed of two desmosomal cadherins: desmocollin (Dsc) and desmoglein (Dsg). Previous studies demonstrate that E-cadherin (Ecad), an adhesive protein that interacts in ... ...

Abstract	Desmosomes are adhesive junctions composed of two desmosomal cadherins: desmocollin (Dsc) and desmoglein (Dsg). Previous studies demonstrate that E-cadherin (Ecad), an adhesive protein that interacts in both
MeSH term(s)	Antigens, CD/metabolism ; Cadherins/metabolism ; Desmoglein 2/metabolism ; Desmosomes/metabolism ; HEK293 Cells ; Humans ; Microscopy, Atomic Force ; Microscopy, Confocal ; Microscopy, Fluorescence ; Protein Binding ; Protein Interaction Mapping ; Protein Multimerization
Chemical Substances	Antigens, CD ; CDH1 protein, human ; Cadherins ; DSG2 protein, human ; Desmoglein 2
Language	English
Publishing date	2018-07-12
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.37629
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Article ; Online: Molecular organization of the desmosome as revealed by direct stochastic optical reconstruction microscopy.

Stahley, Sara N / Bartle, Emily I / Atkinson, Claire E / Kowalczyk, Andrew P / Mattheyses, Alexa L

Journal of cell science

2016 Volume 129, Issue 15, Page(s) 2897–2904

Abstract: ... the organization of desmoglein 3, plakoglobin and desmoplakin (N-terminal, rod and C-terminal domains) in primary ...

Abstract	Desmosomes are macromolecular junctions responsible for providing strong cell-cell adhesion. Because of their size and molecular complexity, the precise ultrastructural organization of desmosomes is challenging to study. Here, we used direct stochastic optical reconstruction microscopy (dSTORM) to resolve individual plaque pairs for inner and outer dense plaque proteins. Analysis methods based on desmosomal mirror symmetry were developed to measure plaque-to-plaque distances and create an integrated map. We quantified the organization of desmoglein 3, plakoglobin and desmoplakin (N-terminal, rod and C-terminal domains) in primary human keratinocytes. Longer desmosome lengths correlated with increasing plaque-to-plaque distance, suggesting that desmoplakin is arranged with its long axis at an angle within the plaque. We next examined whether plaque organization changed in different adhesive states. Plaque-to-plaque distance for the desmoplakin rod and C-terminal domains decreased in PKP-1-mediated hyperadhesive desmosomes, suggesting that protein reorganization correlates with function. Finally, in human epidermis we found a difference in plaque-to-plaque distance for the desmoplakin C-terminal domain, but not the desmoplakin rod domain or plakoglobin, between basal and suprabasal cells. Our data reveal the molecular organization of desmosomes in cultured keratinocytes and skin as defined by dSTORM.
MeSH term(s)	Cell Adhesion ; Desmosomes/metabolism ; Humans ; Male ; Microscopy/methods ; Optical Phenomena ; Plakophilins/metabolism ; Skin/metabolism ; Stochastic Processes
Chemical Substances	Plakophilins
Language	English
Publishing date	2016-08-01
Publishing country	England
Document type	Journal Article
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.185785
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Article ; Online: Desmosome assembly and disassembly are membrane raft-dependent.

Stahley, Sara N / Saito, Masataka / Faundez, Victor / Koval, Michael / Mattheyses, Alexa L / Kowalczyk, Andrew P

PloS one

2014 Volume 9, Issue 1, Page(s) e87809

Abstract: Strong intercellular adhesion is critical for tissues that experience mechanical stress, such as the skin and heart. Desmosomes provide adhesive strength to tissues by anchoring desmosomal cadherins of neighboring cells to the intermediate filament ... ...

Abstract	Strong intercellular adhesion is critical for tissues that experience mechanical stress, such as the skin and heart. Desmosomes provide adhesive strength to tissues by anchoring desmosomal cadherins of neighboring cells to the intermediate filament cytoskeleton. Alterations in assembly and disassembly compromise desmosome function and may contribute to human diseases, such as the autoimmune skin blistering disease pemphigus vulgaris (PV). We previously demonstrated that PV auto-antibodies directed against the desmosomal cadherin desmoglein 3 (Dsg3) cause loss of adhesion by triggering membrane raft-mediated Dsg3 endocytosis. We hypothesized that raft membrane microdomains play a broader role in desmosome homeostasis by regulating the dynamics of desmosome assembly and disassembly. In human keratinocytes, Dsg3 is raft associated as determined by biochemical and super resolution immunofluorescence microscopy methods. Cholesterol depletion, which disrupts rafts, prevented desmosome assembly and adhesion, thus functionally linking rafts to desmosome formation. Interestingly, Dsg3 did not associate with rafts in cells lacking desmosomal proteins. Additionally, PV IgG-induced desmosome disassembly occurred by redistribution of Dsg3 into raft-containing endocytic membrane domains, resulting in cholesterol-dependent loss of adhesion. These findings demonstrate that membrane rafts are required for desmosome assembly and disassembly dynamics, suggesting therapeutic potential for raft targeting agents in desmosomal diseases such as PV.
MeSH term(s)	Cell Adhesion/physiology ; Cell Membrane/metabolism ; Cells, Cultured ; Cholesterol/metabolism ; Desmoglein 3/metabolism ; Endocytosis/physiology ; Humans ; Immunoglobulin G/metabolism ; Keratinocytes/metabolism ; Microscopy, Immunoelectron/methods ; Pemphigus/metabolism
Chemical Substances	DSG3 protein, human ; Desmoglein 3 ; Immunoglobulin G ; Cholesterol (97C5T2UQ7J)
Language	English
Publishing date	2014-01-30
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0087809
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Article ; Online: E-cadherin binds to desmoglein to facilitate desmosome assembly

Omer Shafraz / Matthias Rübsam / Sara N Stahley / Amber L Caldara / Andrew P Kowalczyk / Carien M Niessen / Sanjeevi Sivasankar

eLife, Vol

2018 Volume 7

Abstract	Desmosomes are adhesive junctions composed of two desmosomal cadherins: desmocollin (Dsc) and desmoglein (Dsg). Previous studies demonstrate that E-cadherin (Ecad), an adhesive protein that interacts in both trans (between opposing cells) and cis (on the same cell surface) conformations, facilitates desmosome assembly via an unknown mechanism. Here we use structure-function analysis to resolve the mechanistic roles of Ecad in desmosome formation. Using AFM force measurements, we demonstrate that Ecad interacts with isoform 2 of Dsg via a conserved Leu-175 on the Ecad cis binding interface. Super-resolution imaging reveals that Ecad is enriched in nascent desmosomes, supporting a role for Ecad in early desmosome assembly. Finally, confocal imaging demonstrates that desmosome assembly is initiated at sites of Ecad mediated adhesion, and that Ecad-L175 is required for efficient Dsg2 and desmoplakin recruitment to intercellular contacts. We propose that Ecad trans interactions at nascent cell-cell contacts initiate the recruitment of Dsg through direct cis interactions with Ecad which facilitates desmosome assembly.
Keywords	cell adhesion ; desmosomes ; cadherins ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
Subject code	571
Language	English
Publishing date	2018-07-01T00:00:00Z
Publisher	eLife Sciences Publications Ltd
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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