| Content Provider |
World Health Organization (WHO)-Global Index Medicus |
| Author |
Hamill, Kevin J. Hiroyasu, Sho Colburn, Zachary T. Ventrella, Rosa V. Hopkinson, Susan B. Skalli, Omar Jones, Jonathan C. R. |
| Description |
Country affiliation: United kingdom Author Affiliation: Hamill KJ ( Department of Eye and Vision Science, Institute of Ageing and Chronic Diseases, University of Liverpool, Liverpool, UK.); Hiroyasu S ( School of Molecular Biosciences, Washington State University, Pullman, Washington, USA.); Colburn ZT ( School of Molecular Biosciences, Washington State University, Pullman, Washington, USA.); Ventrella RV ( Department of Dermatology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois, USA.); Hopkinson SB ( School of Molecular Biosciences, Washington State University, Pullman, Washington, USA.); Skalli O ( Department of Biological Sciences, University of Memphis, Memphis, Tennessee, USA.); Jones JC ( School of Molecular Biosciences, Washington State University, Pullman, Washington, USA.) |
| Abstract |
The migration of keratinocytes in wound healing requires coordinated activities of the motility machinery of a cell, the cytoskeleton, and matrix adhesions. In this study, we assessed the role of alpha actinin-1 (ACTN1), one of the two alpha actinin isoforms expressed in keratinocytes, in skin cell migration via a small hairpin RNA-mediated knockdown approach. Keratinocytes deficient in ACTN1 exhibit changes in their actin cytoskeleton organization, a loss in front-rear polarity, and impaired lamellipodial dynamics. They also display aberrant directed motility and move slower compared with their wild-type counterparts. Moreover, they have abnormally arranged matrix adhesion sites. Specifically, the focal adhesions in ACTN1 knockdown keratinocytes are not organized as distinct entities. Rather, focal adhesion proteins are arranged in a circle subjacent to cortical fibers of actin. In the same cells, hemidesmosome proteins arrange in cat paw patterns, more typical of confluent, stationary cells, and ß4 integrin dynamics are reduced in knockdown cells compared with control keratinocytes. In summary, our data suggest a mechanism by which ACTN1 determines the motility of keratinocytes by regulating the organization of the actin cytoskeleton, focal adhesion, and hemidesmosome proteins complexes, thereby modulating cell speed, lamellipodial dynamics, and directed migration. |
| File Format |
HTM / HTML |
| ISSN |
0022202X |
| e-ISSN |
15231747 |
| DOI |
10.1038/jid.2014.505 |
| Journal |
Journal of Investigative Dermatology |
| Issue Number |
4 |
| Volume Number |
135 |
| Language |
English |
| Publisher |
Elsevier |
| Publisher Date |
2015-04-01 |
| Publisher Place |
United States |
| Access Restriction |
Open |
| Subject Keyword |
Discipline Dermatology Actinin Metabolism Keratinocytes Cytology Skin Actins Adenoviridae Cell Movement Cell Separation Cytoskeleton Epidermolysis Bullosa, Junctional Flow Cytometry Hemidesmosomes Integrin Beta4 Pseudopodia Wound Healing Research Support, N.i.h., Extramural |
| Content Type |
Text |
| Resource Type |
Article |
| Subject |
Cell Biology Biochemistry Molecular Biology Dermatology |
