The Actin-Based Motor Myosin Vb Is Crucial to Maintain Epidermal Barrier Integrity

Myosin Vb (Myo5b) is an unconventional myosin involved in the actin-dependent transport and tethering of intracellular organelles. In the epidermis, granular keratinocytes accumulate cytoplasmic lamellar bodies (LBs), secretory vesicles released at the junction with the stratum corneum that particip...

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Bibliographic Details
Published in:Journal of investigative dermatology 2019-07, Vol.139 (7), p.1430-1438
Main Authors: Reynier, Marie, Allart, Sophie, Goudounèche, Dominique, Moga, Alain, Serre, Guy, Simon, Michel, Leprince, Corinne
Format: Article
Language:English
Subjects:
Actin Cytoskeleton - metabolism
Actins - metabolism
Cells, Cultured
Claudin-1 - metabolism
Epidermis - metabolism
Epidermis - pathology
Human health and pathology
Humans
Infectious diseases
Intercellular Signaling Peptides and Proteins - metabolism
Keratinocytes - metabolism
Keratinocytes - pathology
Life Sciences
Myosin Heavy Chains - genetics
Myosin Heavy Chains - metabolism
Myosin Type V - genetics
Myosin Type V - metabolism
Protein Binding
Protein Transport
rab GTP-Binding Proteins - metabolism
RNA, Small Interfering - genetics
Tight Junctions - metabolism
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Summary:Myosin Vb (Myo5b) is an unconventional myosin involved in the actin-dependent transport and tethering of intracellular organelles. In the epidermis, granular keratinocytes accumulate cytoplasmic lamellar bodies (LBs), secretory vesicles released at the junction with the stratum corneum that participate actively in the maintenance of the epidermal barrier. We have previously demonstrated that LB biogenesis is controlled by the Rab11a guanosine triphosphate hydrolase, known for its ability to recruit the Myo5b motor. In order to better characterize the molecular pathway that controls LB trafficking, we analyzed the role of F-actin and Myo5b in the epidermis. We demonstrated that LB distribution in granular keratinocytes was dependent on a dynamic F-actin cytoskeleton. Myo5b was shown to be highly expressed in granular keratinocytes and associated with corneodesmosin-loaded LB. In reconstructed human epidermis, Myo5b silencing led to epidermal barrier defects associated with structural alterations of the stratum corneum and a reduced pool of LB showing signs of disordered maturation. Myo5b depletion also disturbed the expression and distribution of both LB cargoes and junctional components, such as claudin-1, which demonstrates its action on both LB trafficking and junctional complex composition. Together, our data reveal the essential role of Myo5b in maintaining the epidermal barrier integrity.
ISSN:0022-202X
1523-1747
DOI:10.1016/j.jid.2018.12.021