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The molecular architecture of hemidesmosomes, as revealed with super-resolution microscopy
Leila Nahidiazar1, Maaike Kreft1, Bram van den Broek1
1Division of Cell Biology, The Netherlands Cancer Institute, Plesmanlaan 121, Amsterdam 1066 CX, The Netherlands.
Insights
Super-resolution microscopy reveals the molecular architecture of hemidesmosomes. Plectin interacts with integrin β4 and keratin, while BP180 and BP230 form distinct layers within these cell adhesion structures.
Area of Science:
- Cell Biology
- Molecular Biology
- Biophysics
Background:
- Hemidesmosomes are crucial for epithelial cell adhesion and tissue integrity.
- Previous studies using immunofluorescence microscopy had limited resolution, hindering a detailed understanding of hemidesmosome organization.
Purpose of the Study:
- To elucidate the precise molecular organization and architecture of hemidesmosomes using advanced super-resolution microscopy.
- To investigate the spatial relationships between key hemidesmosomal proteins and keratin intermediate filaments.
Main Methods:
- Utilized two- and three-color super-resolution microscopy on cultured keratinocytes.
- Developed innovative methods for quantifying molecular distances within hemidesmosomes.
- Examined hemidesmosome structure in both cultured cells and ex vivo skin cross-sections.
Main Results:
- Observed nascent hemidesmosomes associating with individual keratin filaments, with integrin β4 (ITGB4) located along keratin filaments.
- Demonstrated simultaneous and asymmetric interaction between plectin, integrin β4, and keratin.
- Revealed a distinct arrangement of BP180 (collagen XVII) surrounding a central core of BP230 (dystonin epithelial splice variant) within hemidesmosomes.
- Identified plectin and BP230 positioned between integrin β4 and BP180/keratin system in skin sections.
Conclusions:
- Provided a high-resolution view of hemidesmosome molecular architecture in cultured keratinocytes and skin.
- Detailed the specific spatial arrangement and interactions of key proteins like plectin, integrin β4, BP180, and BP230.
- Advanced the understanding of how hemidesmosomes anchor keratin intermediate filaments to the extracellular matrix.
Abstract:
Hemidesmosomes have been extensively studied with immunofluorescence microscopy, but owing to its limited resolution, the precise organization of hemidesmosomes remains poorly understood. We studied hemidesmosome organization in cultured keratinocytes with two- and three-color super-resolution microscopy. We observed that, in the cell periphery, nascent hemidesmosomes are associated with individual keratin filaments and that β4 integrin (also known as ITGB4) is distributed along, rather than under, keratin filaments. By applying innovative methods to quantify molecular distances, we demonstrate that the hemidesmosomal plaque protein plectin interacts simultaneously and asymmetrically with β4 integrin and keratin. Furthermore, we show that BP180 (BPAG2, also known as collagen XVII) and BP230 (BPAG1e, an epithelial splice variant of dystonin) are characteristically arranged within hemidesmosomes with BP180 surrounding a central core of BP230 molecules. In skin cross-sections, hemidesmosomes of variable sizes could be distinguished with BP230 and plectin occupying a position in between β4 integrin and BP180, and the intermediate filament system. In conclusion, our data provide a detailed view of the molecular architecture of hemidesmosomes in cultured keratinocytes and skin.
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