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
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1141721
- author
- Navdaev, Alexei ; Heitmann, Vanessa ; Desantana Evangelista, Karla ; Mörgelin, Matthias LU ; Wegener, Joachim and Eble, Johannes A
- organization
- publishing date
- 2008
- 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
- pmid:18045589
- 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
- 2016-04-01 12:22:41
- date last changed
- 2022-01-27 02:54:16
@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}},
keywords = {{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}},
doi = {{10.1016/j.yexcr.2007.10.027}},
volume = {{314}},
year = {{2008}},
}