Abstract
Paxillin is a cytoskeletal protein found in structures of focal adhesions where cells adhere to the extracellular matrix. We isolated paxillin cDNA from the Xenopus laevis ovary. The cDNA sequence encodes a protein of 539 amino acids with four LIM and five LD motifs. 80% of the amino acids of frog paxillin are shared by human and chicken paxillins. Northern analysis showed that the frog gene is expressed in the spleen, kidney, testis and ovary. Immunocytochemistry showed that paxillin protein is accumulated in the nucleus as well as in the periphery of the cytoplasm of the A6 cell. This intriguing result shows that paxillin, which has been characterized as a cytoskeletal protein, is capable of translocating to the nucleus.
| Original language | English |
|---|---|
| Pages (from-to) | 235-240 |
| Number of pages | 6 |
| Journal | Biochimica et Biophysica Acta - Gene Structure and Expression |
| Volume | 1519 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 2001 Jun 28 |
Keywords
- LIM motif
- Nuclear export signal
- Nuclear translocation
- Paxillin
- Xenopus laevis
ASJC Scopus subject areas
- Structural Biology
- Biophysics
- Biochemistry
- Genetics
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Cite this
Ogawa, M., Hiraoka, Y., Taniguchi, K., Sakai, Y., & Aiso, S. (2001). mRNA sequence of the Xenopus laevis paxillin gene and its expression. Biochimica et Biophysica Acta - Gene Structure and Expression, 1519(3), 235-240. https://doi.org/10.1016/S0167-4781(01)00230-5