Cell-cell adhesion and RhoA-mediated actin polymerization are independent phenomena in microtubule disrupted keratinocytes.
E-cadherin-mediated adherens junction formation and maintenance are thought to involve actin filament rearrangements through the action of small GTPases. Recently, we demonstrated that microtubule disruption in normal human epidermal keratinocytes grown in low calcium media conditions induces cell-cell adhesion by redistribution of endogenous E-cadherin, and it promotes stress fiber formation. This actin rearrangement was apparently mediated by RhoA activation. This model system therefore provides a tool with which to dissect relationships between cell-cell adhesion and Rho-mediated stress fiber formation. In this study, we have demonstrated in normal human epidermal keratinocytes that disruption of actin structures including stress fibers does not interfere with E-cadherin redistribution during microtubule-induced cell-cell adhesion. Moreover, this cell-cell adhesion could not be blocked by RhoA inactivation at the level for inhibition of stress fiber formation. Additionally, in the immortalized HaCaT keratinocyte cell line, which does not undergo cell-cell adhesion after microtubule disruption in low calcium conditions, expression of dominant-active RhoA could induce stress fiber formation without inducing adhesion. On the other hand, a variant of the HaCaT cell line, HC-R1, showed microtubule-disruption-induced cell-cell adhesion without stress fiber formation. Together, our results suggest that, in keratinocytes, the process of cell adhesion can occur independently of RhoA-mediated stress fiber formation.
Laboratory of Skin Biology, National Institute of Arthritis, Musculoskeletal and Skin Diseases, Bethesda, Maryland 20892-8023, USA.
Sun-Ho
SH
Kee
Shyh-Ing
SI
Jang
Bijan
B
Ahvazi
Melinda
M
Larsen
Kenneth M
KM
Yamada
Peter M
PM
Steinert
D000199:Actins / Q000378:metabolism*; D015820:Cadherins / Q000502:physiology; D002448:Cell Adhesion / Q000187:drug effects; D002478:Cells, Cultured; D006801:Humans; D015603:Keratinocytes / Q000502:physiology*; D008870:Microtubules / Q000502:physiology*; D009355:Neomycin / Q000494:pharmacology; D015739:Nocodazole / Q000494:pharmacology; D011108:Polymers / Q000378:metabolism; D022502:Stress Fibers / Q000502:physiology; D020742:rhoA GTP-Binding Protein / Q000502:physiology*
D000199:Actins; D015820:Cadherins; D011108:Polymers; D020742:rhoA GTP-Binding Protein; D009355:Neomycin; D015739:Nocodazole