Tenascin-C suppresses Rho activation.
Cell binding to extracellular matrix (ECM) components changes cytoskeletal organization by the activation of Rho family GTPases. Tenascin-C, a developmentally regulated matrix protein, modulates cellular responses to other matrix proteins, such as fibronectin (FN). Here, we report that tenascin-C ma...
| Główni autorzy: | , , |
|---|---|
| Format: | Journal article |
| Język: | English |
| Wydane: |
2000
|
| _version_ | 1826305601156677632 |
|---|---|
| author | Wenk, M Midwood, K Schwarzbauer, J |
| author_facet | Wenk, M Midwood, K Schwarzbauer, J |
| author_sort | Wenk, M |
| collection | OXFORD |
| description | Cell binding to extracellular matrix (ECM) components changes cytoskeletal organization by the activation of Rho family GTPases. Tenascin-C, a developmentally regulated matrix protein, modulates cellular responses to other matrix proteins, such as fibronectin (FN). Here, we report that tenascin-C markedly altered cell phenotype on a three-dimensional fibrin matrix containing FN, resulting in suppression of actin stress fibers and induction of actin-rich filopodia. This distinct morphology was associated with complete suppression of the activation of RhoA, a small GTPase that induces actin stress fiber formation. Enforced activation of RhoA circumvented the effects of tenascin. Effects of active Rho were reversed by a Rho inhibitor C3 transferase. Suppression of GTPase activation allows tenascin-C expression to act as a regulatory switch to reverse the effects of adhesive proteins on Rho function. This represents a novel paradigm for the regulation of cytoskeletal organization by ECM. |
| first_indexed | 2024-03-07T06:35:18Z |
| format | Journal article |
| id | oxford-uuid:f76ab66e-d0e9-4694-8d94-9d4049faa57f |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T06:35:18Z |
| publishDate | 2000 |
| record_format | dspace |
| spelling | oxford-uuid:f76ab66e-d0e9-4694-8d94-9d4049faa57f2022-03-27T12:42:29ZTenascin-C suppresses Rho activation.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:f76ab66e-d0e9-4694-8d94-9d4049faa57fEnglishSymplectic Elements at Oxford2000Wenk, MMidwood, KSchwarzbauer, JCell binding to extracellular matrix (ECM) components changes cytoskeletal organization by the activation of Rho family GTPases. Tenascin-C, a developmentally regulated matrix protein, modulates cellular responses to other matrix proteins, such as fibronectin (FN). Here, we report that tenascin-C markedly altered cell phenotype on a three-dimensional fibrin matrix containing FN, resulting in suppression of actin stress fibers and induction of actin-rich filopodia. This distinct morphology was associated with complete suppression of the activation of RhoA, a small GTPase that induces actin stress fiber formation. Enforced activation of RhoA circumvented the effects of tenascin. Effects of active Rho were reversed by a Rho inhibitor C3 transferase. Suppression of GTPase activation allows tenascin-C expression to act as a regulatory switch to reverse the effects of adhesive proteins on Rho function. This represents a novel paradigm for the regulation of cytoskeletal organization by ECM. |
| spellingShingle | Wenk, M Midwood, K Schwarzbauer, J Tenascin-C suppresses Rho activation. |
| title | Tenascin-C suppresses Rho activation. |
| title_full | Tenascin-C suppresses Rho activation. |
| title_fullStr | Tenascin-C suppresses Rho activation. |
| title_full_unstemmed | Tenascin-C suppresses Rho activation. |
| title_short | Tenascin-C suppresses Rho activation. |
| title_sort | tenascin c suppresses rho activation |
| work_keys_str_mv | AT wenkm tenascincsuppressesrhoactivation AT midwoodk tenascincsuppressesrhoactivation AT schwarzbauerj tenascincsuppressesrhoactivation |