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The C-terminus of the gamma2 chain but not of the beta3 chain of laminin-332 is indirectly but indispensably necessary for integrin-mediated cell reactions

Navdaev, Alexei; Heitmann, Vanessa; Desantana Evangelista, Karla; Mörgelin, Matthias LU ; Wegener, Joachim and Eble, Johannes A (2008) In Experimental Cell Research 314(3). p.489-497
Abstract
Using a recombinant mini-laminin-332, we showed that truncation of the three C-terminal amino acids of the gamma2 chain, but not of the C-terminal amino acid of the beta3 chain, completely abolished alpha3beta1 integrin binding and its cellular functions, such as attachment and spreading. However, a synthetic peptide mimicking the gamma2 chain C-terminus did not interfere with alpha3beta1 integrin binding or cell adhesion and spreading on laminin-332 as measured by protein interaction assays and electric cell-substrate impedance sensing. Nor was the soluble peptide able to restore the loss of integrin-mediated cell adhesiveness to mini-laminin-332 after deletion of the gamma2 chain C-terminus. These findings spoke against the hypothesis... (More)
Using a recombinant mini-laminin-332, we showed that truncation of the three C-terminal amino acids of the gamma2 chain, but not of the C-terminal amino acid of the beta3 chain, completely abolished alpha3beta1 integrin binding and its cellular functions, such as attachment and spreading. However, a synthetic peptide mimicking the gamma2 chain C-terminus did not interfere with alpha3beta1 integrin binding or cell adhesion and spreading on laminin-332 as measured by protein interaction assays and electric cell-substrate impedance sensing. Nor was the soluble peptide able to restore the loss of integrin-mediated cell adhesiveness to mini-laminin-332 after deletion of the gamma2 chain C-terminus. These findings spoke against the hypothesis that the gamma2 chain C-terminus of laminin-332 is a part of the alpha3beta1 integrin interaction site. In addition, structural studies with electron microscopy showed that truncation of the gamma2 chain C-terminus opened up the compact supradomain structure of LG1-3 domains. Thus, by inducing or stabilizing an integrin binding-competent conformation or array of the LG1-3 domains, the gamma2 chain C-terminus plays an indirect but essential role in laminin-332 recognition by alpha3beta1 integrin and, hence, its cellular functions. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Adhesion, Epithelial cell layer, Recognition site, ECIS
in
Experimental Cell Research
volume
314
issue
3
pages
489 - 497
publisher
Academic Press
external identifiers
  • pmid:18045589
  • wos:000252832300007
  • scopus:38149046456
ISSN
1090-2422
DOI
10.1016/j.yexcr.2007.10.027
language
English
LU publication?
yes
id
433e495a-65f0-4bc8-b279-d60e6c5900d3 (old id 1141721)
date added to LUP
2008-08-12 10:35:46
date last changed
2017-07-30 03:49:10
@article{433e495a-65f0-4bc8-b279-d60e6c5900d3,
  abstract     = {Using a recombinant mini-laminin-332, we showed that truncation of the three C-terminal amino acids of the gamma2 chain, but not of the C-terminal amino acid of the beta3 chain, completely abolished alpha3beta1 integrin binding and its cellular functions, such as attachment and spreading. However, a synthetic peptide mimicking the gamma2 chain C-terminus did not interfere with alpha3beta1 integrin binding or cell adhesion and spreading on laminin-332 as measured by protein interaction assays and electric cell-substrate impedance sensing. Nor was the soluble peptide able to restore the loss of integrin-mediated cell adhesiveness to mini-laminin-332 after deletion of the gamma2 chain C-terminus. These findings spoke against the hypothesis that the gamma2 chain C-terminus of laminin-332 is a part of the alpha3beta1 integrin interaction site. In addition, structural studies with electron microscopy showed that truncation of the gamma2 chain C-terminus opened up the compact supradomain structure of LG1-3 domains. Thus, by inducing or stabilizing an integrin binding-competent conformation or array of the LG1-3 domains, the gamma2 chain C-terminus plays an indirect but essential role in laminin-332 recognition by alpha3beta1 integrin and, hence, its cellular functions.},
  author       = {Navdaev, Alexei and Heitmann, Vanessa and Desantana Evangelista, Karla and Mörgelin, Matthias and Wegener, Joachim and Eble, Johannes A},
  issn         = {1090-2422},
  keyword      = {Adhesion,Epithelial cell layer,Recognition site,ECIS},
  language     = {eng},
  number       = {3},
  pages        = {489--497},
  publisher    = {Academic Press},
  series       = {Experimental Cell Research},
  title        = {The C-terminus of the gamma2 chain but not of the beta3 chain of laminin-332 is indirectly but indispensably necessary for integrin-mediated cell reactions},
  url          = {http://dx.doi.org/10.1016/j.yexcr.2007.10.027},
  volume       = {314},
  year         = {2008},
}