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The PET and LIM1-2 domains of testin contribute to intramolecular and homodimeric interactions

(2017) PLOS ONE. 12(5).
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Abstract
The focal adhesion protein testin is a modular scaffold and tumour suppressor that consists of an N-terminal cysteine rich (CR) domain, a PET domain of unknown function and three C-terminal LIM domains. Testin has been proposed to have an open and a closed conformation based on the observation that its N-terminal half and C-terminal half directly interact. Here we extend the testin conformational model by demonstrating that testin can also form an antiparallel homodimer. In support of this extended model we determined that the testin region (amino acids 52-233) harbouring the PET domain interacts with the C-terminal LIM1-2 domains in vitro and in cells, and assign a critical role to tyrosine 288 in this interaction.
Keywords
FOCAL ADHESION PROTEIN, TUMOR-SUPPRESSOR, ACTIN, BINDING, VINCULIN, CANCER, ZYXIN, BREAST, GENE, EVL

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Citation

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Chicago
Sala, Stefano, Marie Catillon, Ermin Hadzic, Elisabeth Schaffner-Reckinger, Marleen Van Troys, and Christophe Ampe. 2017. “The PET and LIM1-2 Domains of Testin Contribute to Intramolecular and Homodimeric Interactions.” Plos One 12 (5).
APA
Sala, S., Catillon, M., Hadzic, E., Schaffner-Reckinger, E., Van Troys, M., & Ampe, C. (2017). The PET and LIM1-2 domains of testin contribute to intramolecular and homodimeric interactions. PLOS ONE, 12(5).
Vancouver
1.
Sala S, Catillon M, Hadzic E, Schaffner-Reckinger E, Van Troys M, Ampe C. The PET and LIM1-2 domains of testin contribute to intramolecular and homodimeric interactions. PLOS ONE. 2017;12(5).
MLA
Sala, Stefano, Marie Catillon, Ermin Hadzic, et al. “The PET and LIM1-2 Domains of Testin Contribute to Intramolecular and Homodimeric Interactions.” PLOS ONE 12.5 (2017): n. pag. Print.
@article{8524213,
  abstract     = {The focal adhesion protein testin is a modular scaffold and tumour suppressor that consists of an N-terminal cysteine rich (CR) domain, a PET domain of unknown function and three C-terminal LIM domains. Testin has been proposed to have an open and a closed conformation based on the observation that its N-terminal half and C-terminal half directly interact. Here we extend the testin conformational model by demonstrating that testin can also form an antiparallel homodimer. In support of this extended model we determined that the testin region (amino acids 52-233) harbouring the PET domain interacts with the C-terminal LIM1-2 domains in vitro and in cells, and assign a critical role to tyrosine 288 in this interaction.},
  articleno    = {e0177879},
  author       = {Sala, Stefano and Catillon, Marie and Hadzic, Ermin and Schaffner-Reckinger, Elisabeth and Van Troys, Marleen and Ampe, Christophe},
  issn         = {1932-6203},
  journal      = {PLOS ONE},
  keyword      = {FOCAL ADHESION PROTEIN,TUMOR-SUPPRESSOR,ACTIN,BINDING,VINCULIN,CANCER,ZYXIN,BREAST,GENE,EVL},
  language     = {eng},
  number       = {5},
  pages        = {21},
  title        = {The PET and LIM1-2 domains of testin contribute to intramolecular and homodimeric interactions},
  url          = {http://dx.doi.org/10.1371/journal.pone.0177879},
  volume       = {12},
  year         = {2017},
}

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