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

Stefano Sala UGent, Marie Catillon, Ermin Hadzic, Elisabeth Schaffner-Reckinger, Marleen Van Troys UGent and Christophe Ampe UGent (2017) PLOS ONE. 12(5).
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.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
FOCAL ADHESION PROTEIN, TUMOR-SUPPRESSOR, ACTIN, BINDING, VINCULIN, CANCER, ZYXIN, BREAST, GENE, EVL
journal title
PLOS ONE
PLoS One
volume
12
issue
5
article number
e0177879
pages
21 pages
Web of Science type
Article
Web of Science id
000401672400106
ISSN
1932-6203
DOI
10.1371/journal.pone.0177879
language
English
UGent publication?
yes
classification
A1
additional info
the last two authors contributed equally to this work
copyright statement
I have retained and own the full copyright for this publication
id
8524213
handle
http://hdl.handle.net/1854/LU-8524213
date created
2017-06-19 12:44:18
date last changed
2017-06-22 07:50:15
@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},
}

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.