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Article ; Online: Retromer Chaperones: Potential Therapeutics for Treatment of Skin Disease?

Hegazy, Marihan / Green, Kathleen J

The Journal of investigative dermatology

2023 Volume 143, Issue 9, Page(s) 1634–1637

MeSH term(s)	Humans ; Molecular Chaperones/therapeutic use ; Protein Transport ; Skin Diseases/drug therapy ; Skin Diseases/metabolism ; Endosomes/metabolism
Chemical Substances	Molecular Chaperones
Language	English
Publishing date	2023-06-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	80136-7
ISSN	1523-1747 ; 0022-202X
ISSN (online)	1523-1747
ISSN	0022-202X
DOI	10.1016/j.jid.2023.05.003
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Ui VI Zs.124: Show issues

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Article ; Online: Plectin pulls it together, coupling the cortical actin and intermediate filament cytoskeletons.

Broussard, Joshua A / Green, Kathleen J

The Journal of cell biology

2022 Volume 221, Issue 3

Abstract: ... In this issue, Prechova et al. (2022. J. Cell Biol.https://doi.org/10.1083/jcb.202105146) demonstrate ...

Abstract	The integration of cytoskeletal/adhesive networks is critical to epithelial mechanobiology. In this issue, Prechova et al. (2022. J. Cell Biol.https://doi.org/10.1083/jcb.202105146) demonstrate that the cytolinker protein plectin is essential for the construction of a cortical cytoskeletal architecture required for epithelial tensional homeostasis.
MeSH term(s)	Actins/metabolism ; Cytoskeleton/metabolism ; Intermediate Filaments/metabolism ; Plectin/genetics ; Plectin/metabolism
Chemical Substances	Actins ; Plectin
Language	English
Publishing date	2022-02-17
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Comment
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202201054
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Article ; Online: PP2A-B55alpha controls keratinocyte adhesion through dephosphorylation of the Desmoplakin C-terminus.

Perl, Abbey L / Koetsier, Jennifer L / Green, Kathleen J

Scientific reports

2023 Volume 13, Issue 1, Page(s) 12720

Abstract: Critical for the maintenance of epidermal integrity and function are attachments between intermediate filaments (IF) and intercellular junctions called desmosomes. The desmosomal cytoplasmic plaque protein desmoplakin (DP) is essential for anchoring IF ... ...

Abstract	Critical for the maintenance of epidermal integrity and function are attachments between intermediate filaments (IF) and intercellular junctions called desmosomes. The desmosomal cytoplasmic plaque protein desmoplakin (DP) is essential for anchoring IF to the junction. DP-IF interactions are regulated by a phospho-regulatory motif within the DP C-terminus controlling keratinocyte intercellular adhesion. Here we identify the protein phosphatase 2A (PP2A)-B55α holoenzyme as the major serine/threonine phosphatase regulating DP's C-terminus and consequent intercellular adhesion. Using a combination of chemical and genetic approaches, we show that the PP2A-B55α holoenzyme interacts with DP at intercellular membranes in 2D- and 3D- epidermal models and human skin samples. Our experiments demonstrate that PP2A-B55α regulates the phosphorylation status of junctional DP and is required for maintaining strong desmosome-mediated intercellular adhesion. These data identify PP2A-B55α as part of a regulatory module capable of tuning intercellular adhesion strength and a candidate disease target in desmosome-related disorders of the skin and heart.
MeSH term(s)	Humans ; Desmoplakins ; Holoenzymes/metabolism ; Intercellular Junctions/metabolism ; Keratinocytes/metabolism ; Protein Phosphatase 2/metabolism
Chemical Substances	Desmoplakins ; Holoenzymes ; Protein Phosphatase 2 (EC 3.1.3.16) ; PPP2R2A protein, human
Language	English
Publishing date	2023-08-05
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-023-37874-8
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Article ; Online: PP2A-B55alpha controls keratinocyte adhesion through dephosphorylation of the Desmoplakin C-terminus

Abbey L. Perl / Jennifer L. Koetsier / Kathleen J. Green

Scientific Reports, Vol 13, Iss 1, Pp 1-

2023 Volume 12

Abstract: Abstract Critical for the maintenance of epidermal integrity and function are attachments between intermediate filaments (IF) and intercellular junctions called desmosomes. The desmosomal cytoplasmic plaque protein desmoplakin (DP) is essential for ... ...

Abstract	Abstract Critical for the maintenance of epidermal integrity and function are attachments between intermediate filaments (IF) and intercellular junctions called desmosomes. The desmosomal cytoplasmic plaque protein desmoplakin (DP) is essential for anchoring IF to the junction. DP-IF interactions are regulated by a phospho-regulatory motif within the DP C-terminus controlling keratinocyte intercellular adhesion. Here we identify the protein phosphatase 2A (PP2A)-B55α holoenzyme as the major serine/threonine phosphatase regulating DP’s C-terminus and consequent intercellular adhesion. Using a combination of chemical and genetic approaches, we show that the PP2A-B55α holoenzyme interacts with DP at intercellular membranes in 2D- and 3D- epidermal models and human skin samples. Our experiments demonstrate that PP2A-B55α regulates the phosphorylation status of junctional DP and is required for maintaining strong desmosome-mediated intercellular adhesion. These data identify PP2A-B55α as part of a regulatory module capable of tuning intercellular adhesion strength and a candidate disease target in desmosome-related disorders of the skin and heart.
Keywords	Medicine ; R ; Science ; Q
Subject code	571
Language	English
Publishing date	2023-08-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article: Desmosome-anchored intermediate filaments facilitate tension-sensitive RhoA signaling for epithelial homeostasis.

Nanavati, Bageshri Naimish / Noordstra, Ivar / Verma, Suzie / Duszyc, Kinga / Green, Kathleen J / Yap, Alpha S

bioRxiv : the preprint server for biology

2023

Abstract: Epithelia are subject to diverse forms of mechanical stress during development and post-embryonic life. They possess multiple mechanisms to preserve tissue integrity against tensile forces, which characteristically involve specialized cell-cell adhesion ... ...

Abstract	Epithelia are subject to diverse forms of mechanical stress during development and post-embryonic life. They possess multiple mechanisms to preserve tissue integrity against tensile forces, which characteristically involve specialized cell-cell adhesion junctions coupled to the cytoskeleton. Desmosomes connect to intermediate filaments (IF) via desmoplakin (DP)
Language	English
Publishing date	2023-02-23
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.02.23.529786
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Article ; Online: A user's guide to degradation testing of polyethylene glycol-based hydrogels: From in vitro to in vivo studies.

Rodriguez-Rivera, Gabriel J / Green, Mykel / Shah, Vani / Leyendecker, Kathleen / Cosgriff-Hernandez, Elizabeth

Journal of biomedical materials research. Part A

2023

Abstract: Poly(ethylene glycol) (PEG)-based hydrogels have gained significant attention in the field of biomedical applications due to their versatility and antifouling properties. Acrylate-derivatized PEG hydrogels (PEGDA) are some of the most widely studied ... ...

Abstract	Poly(ethylene glycol) (PEG)-based hydrogels have gained significant attention in the field of biomedical applications due to their versatility and antifouling properties. Acrylate-derivatized PEG hydrogels (PEGDA) are some of the most widely studied hydrogels; however, there has been debate around the degradation mechanism and predicting resorption rates. Several factors influence the degradation rate of PEG hydrogels, including backbone and endgroup chemistry, macromer molecular weight, and polymer concentration. In addition to hydrogel parameters, it is necessary to understand the influence of biological and environmental conditions (e.g., pH and temperature) on hydrogel degradation. Rigorous methods for monitoring degradation in both in vitro and in vivo settings are also critical to hydrogel design and development. Herein, we provide guidance on tailoring PEG hydrogel chemistry to achieve target hydrolytic degradation kinetics for both resorbable and biostable applications. A detailed overview of accelerated testing methods and hydrogel degradation characterization is provided to aid researchers in experimental design and interpreting in vitro-in vivo correlations necessary for predicting hydrogel device performance.
Language	English
Publishing date	2023-09-15
Publishing country	United States
Document type	Journal Article
ZDB-ID	2099989-6
ISSN	1552-4965 ; 1549-3296 ; 0021-9304
ISSN (online)	1552-4965
ISSN	1549-3296 ; 0021-9304
DOI	10.1002/jbm.a.37609
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Zs.A 6195: Show issues

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Article ; Online: Desmosomal Cadherins in Health and Disease.

Hegazy, Marihan / Perl, Abbey L / Svoboda, Sophia A / Green, Kathleen J

Annual review of pathology

2021 Volume 17, Page(s) 47–72

Abstract: Desmosomal cadherins are a recent evolutionary innovation that make up the adhesive core of highly specialized intercellular junctions called desmosomes. Desmosomal cadherins, which are grouped into desmogleins and desmocollins, are related to the ... ...

Abstract	Desmosomal cadherins are a recent evolutionary innovation that make up the adhesive core of highly specialized intercellular junctions called desmosomes. Desmosomal cadherins, which are grouped into desmogleins and desmocollins, are related to the classical cadherins, but their cytoplasmic domains are tailored for anchoring intermediate filaments instead of actin to sites of cell-cell adhesion. The resulting junctions are critical for resisting mechanical stress in tissues such as the skin and heart. Desmosomal cadherins also act as signaling hubs that promote differentiation and facilitate morphogenesis, creating more complex and effective tissue barriers in vertebrate tissues. Interference with desmosomal cadherin adhesive and supra-adhesive functions leads to a variety of autoimmune, hereditary, toxin-mediated, and malignant diseases. We review our current understanding of how desmosomal cadherins contribute to human health and disease, highlight gaps in our knowledge about their regulation and function, and introduce promising new directions toward combatting desmosome-related diseases.
MeSH term(s)	Cadherins/physiology ; Cell Adhesion/physiology ; Desmocollins ; Desmosomes/physiology ; Humans ; Signal Transduction
Chemical Substances	Cadherins ; Desmocollins
Language	English
Publishing date	2021-08-23
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2227429-7
ISSN	1553-4014 ; 1553-4006
ISSN (online)	1553-4014
ISSN	1553-4006
DOI	10.1146/annurev-pathol-042320-092912
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Se 2169: Show issues

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Article: Crosstalk in skin: Loss of desmoglein 1 in keratinocytes inhibits BRAF

Tong, Xin / Burks, Hope E / Ren, Ziyou / Koetsier, Jennifer L / Roth-Carter, Quinn R / Green, Kathleen J

bioRxiv : the preprint server for biology

2023

Abstract: Melanoma arises from transformation of melanocytes in the basal layer of the epidermis where they are surrounded by keratinocytes, with which they interact through cell contact and paracrine communication. Considerable effort has been devoted to ... ...

Abstract	Melanoma arises from transformation of melanocytes in the basal layer of the epidermis where they are surrounded by keratinocytes, with which they interact through cell contact and paracrine communication. Considerable effort has been devoted to determining how the accumulation of oncogene and tumor suppressor gene mutations in melanocytes drive melanoma development. However, the extent to which alterations in keratinocytes that occur in the developing tumor niche serve as extrinsic drivers of melanoma initiation and progression is poorly understood. We recently identified the keratinocyte-specific cadherin, desmoglein 1 (Dsg1), as an important mediator of keratinocyte:melanoma cell crosstalk, demonstrating that its chronic loss, which can occur through melanoma cell-dependent paracrine signaling, promotes behaviors that mimic a malignant phenotype. Here we address the extent to which Dsg1 loss affects early steps in melanomagenesis. RNA-Seq analysis revealed that paracrine signals from Dsg1-deficient keratinocytes mediate a transcriptional switch from a differentiated to undifferentiated cell state in melanocytes expressing BRAF
Language	English
Publishing date	2023-02-17
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.02.16.528886
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Article ; Online: Plakophilin 3 and Par3 facilitate desmosomes' association with the apical junctional complex.

Indra, Indrajyoti / Troyanovsky, Regina B / Green, Kathleen J / Troyanovsky, Sergey M

Molecular biology of the cell

2021 Volume 32, Issue 19, Page(s) 1824–1837

Abstract: Desmosomes (DSMs), together with adherens junctions (AJs) and tight junctions (TJs), constitute the apical cell junctional complex (AJC). While the importance of the apical and basolateral polarity machinery in the organization of AJs and TJs is well ... ...

Abstract	Desmosomes (DSMs), together with adherens junctions (AJs) and tight junctions (TJs), constitute the apical cell junctional complex (AJC). While the importance of the apical and basolateral polarity machinery in the organization of AJs and TJs is well established, how DSMs are positioned within the AJC is not understood. Here we use highly polarized DLD1 cells as a model to address how DSMs integrate into the AJC. We found that knockout (KO) of the desmosomal ARM protein Pkp3, but not other major DSM proteins, uncouples DSMs from the AJC without blocking DSM assembly. DLD1 cells also exhibit a prominent extraDSM pool of Pkp3, concentrated in tricellular (tC) contacts. Probing distinct apicobasal polarity pathways revealed that neither the DSM's association with AJC nor the extraDSM pool of Pkp3 are abolished in cells with defects in Scrib module proteins responsible for basolateral membrane development. However, a loss of the apical polarity protein, Par3, completely eliminates the extraDSM pool of Pkp3 and disrupts AJC localization of desmosomes, dispersing these junctions along the entire length of cell-cell contacts. Our data are consistent with a model whereby Par3 facilitates DSM assembly within the AJC, controlling the availability of an assembly competent pool of Pkp3 stored in tC contacts.
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Adherens Junctions/genetics ; Adherens Junctions/metabolism ; Animals ; Caco-2 Cells ; Cell Communication/genetics ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Cell Line, Tumor ; Cell Polarity/genetics ; Cells, Cultured ; Desmosomes/genetics ; Desmosomes/metabolism ; Dogs ; Epithelial Cells/metabolism ; Gene Knockout Techniques ; Humans ; Madin Darby Canine Kidney Cells ; Microscopy, Fluorescence/methods ; Plakophilins/genetics ; Plakophilins/metabolism ; Tight Junctions/genetics ; Tight Junctions/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Cell Cycle Proteins ; PARD3 protein, human ; PKP3 protein, human ; Plakophilins
Language	English
Publishing date	2021-07-14
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E21-01-0001
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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: Desmosomes polarize and integrate chemical and mechanical signaling to govern epidermal tissue form and function.

Broussard, Joshua A / Koetsier, Jennifer L / Hegazy, Marihan / Green, Kathleen J

Current biology : CB

2021 Volume 31, Issue 15, Page(s) 3275–3291.e5

Abstract: The epidermis is a stratified epithelium in which structural and functional features are polarized across multiple cell layers. This type of polarity is essential for establishing the epidermal barrier, but how it is created and sustained is poorly ... ...

Abstract	The epidermis is a stratified epithelium in which structural and functional features are polarized across multiple cell layers. This type of polarity is essential for establishing the epidermal barrier, but how it is created and sustained is poorly understood. Previous work identified a role for the classic cadherin/filamentous-actin network in establishment of epidermal polarity. However, little is known about potential roles of the most prominent epidermal intercellular junction, the desmosome, in establishing epidermal polarity, in spite of the fact that desmosome constituents are patterned across the apical to basal cell layers. Here, we show that desmosomes and their associated intermediate filaments (IFs) are key regulators of mechanical polarization in epidermis, whereby basal and suprabasal cells experience different forces that drive layer-specific functions. Uncoupling desmosomes and IF or specific targeting of apical desmosomes through depletion of the superficial desmosomal cadherin, desmoglein 1, impedes basal stratification in an in vitro competition assay and suprabasal tight junction barrier functions in 3D reconstructed epidermis. Surprisingly, disengaging desmosomes from IF also accelerated the expression of differentiation markers, through precocious activation of the mechanosensitive transcriptional regulator serum response factor (SRF) and downstream activation of epidermal growth factor receptor family member ErbB2 by Src family kinase (SFK)-mediated phosphorylation. This Dsg1-SFK-ErbB2 axis also helps maintain tight junctions and barrier function later in differentiation. Together, these data demonstrate that the desmosome-IF network is a critical contributor to the cytoskeletal-adhesive machinery that supports the polarized function of the epidermis.
MeSH term(s)	Cadherins ; Desmoplakins ; Desmosomes/physiology ; Epidermal Cells ; Epidermis/physiology
Chemical Substances	Cadherins ; Desmoplakins
Language	English
Publishing date	2021-06-08
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2021.05.021
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