Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
Volume 1793, Issue 10, Pages 1588-1596Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamcr.2009.07.007
Keywords
Thioredoxin reductase; Cytoskeleton; Actin; Filopodia
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Funding
- Swedish Cancer Society
- Swedish Research Council [K99-13X-10370]
- Knut and Alice Wallenberg Foundations
- Karolinska Institutet
- Spanish Ministry of Science
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Thioredoxin reductases are important selenoproteins maintaining cellular redox balance and regulating several redox dependent processes in apoptosis, cell proliferation and differentiation. Specific functions of dedicated splice variants may add further complexity to the functions of these proteins. We show here that a splice variant of human thioredoxin reductase 1, TXNRD1_v3, forms both dynamic cytoplasmic filaments and provokes instantaneous formation of dynamic cell membrane protrusions identified as filopodia. Using truncated versions of the protein we found that both the cytoplasmic filaments and the filopodia formation were exclusively dependent on the glutaredoxin domain of the protein. Interestingly, actin polymerization was required for filopodia formation triggered by T-XNRD1_v3, but not for generation of cytoplasmic filaments. We conclude that the glutaredoxin domain of TXNRD1_v3 is an atypical regulator of the cell cytoskeleton that potently induces formation of highly ordered cytoplasmic filaments and cell membrane filopodia. (C) 2009 Elsevier B.V. All rights reserved.
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