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Diverging functions among calreticulin isoforms in higher plants.

Thelin, Lisa LU ; Mutwil, Marek; Sommarin, Marianne LU and Persson, Staffan LU (2011) In Plant Signalling & Behavior 6(6). p.905-910
Abstract
The ER chaperone calreticulin plays vital roles in numerous cellular processes, including Ca2+-homeostasis, apoptosis, and cell adhesion, in animal cells. Although calreticulin has been systematically characterized in animal cells, the focus has been on one of the isoforms. However, recent advances in the plant calreticulin field have revealed functional divergence of calreticulin isoforms. While two of the plant isoforms appear to work within a general ER chaperone framework, the third isoform is associated with folding of receptors for brassinosteroids and bacterial peptides. Hence, the discovery of functional specialization of plant calreticulins opens up new vistas for calreticulins also in the animal field.
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Plant Signalling & Behavior
volume
6
issue
6
pages
905 - 910
publisher
Landes Bioscience
external identifiers
  • pmid:21586899
  • scopus:79958251812
ISSN
1559-2316
language
English
LU publication?
yes
id
a2577856-2b50-4620-86c0-d07051f96cca (old id 1972423)
date added to LUP
2011-06-17 12:54:47
date last changed
2017-09-24 03:18:22
@article{a2577856-2b50-4620-86c0-d07051f96cca,
  abstract     = {The ER chaperone calreticulin plays vital roles in numerous cellular processes, including Ca2+-homeostasis, apoptosis, and cell adhesion, in animal cells. Although calreticulin has been systematically characterized in animal cells, the focus has been on one of the isoforms. However, recent advances in the plant calreticulin field have revealed functional divergence of calreticulin isoforms. While two of the plant isoforms appear to work within a general ER chaperone framework, the third isoform is associated with folding of receptors for brassinosteroids and bacterial peptides. Hence, the discovery of functional specialization of plant calreticulins opens up new vistas for calreticulins also in the animal field.},
  author       = {Thelin, Lisa and Mutwil, Marek and Sommarin, Marianne and Persson, Staffan},
  issn         = {1559-2316},
  language     = {eng},
  number       = {6},
  pages        = {905--910},
  publisher    = {Landes Bioscience},
  series       = {Plant Signalling & Behavior},
  title        = {Diverging functions among calreticulin isoforms in higher plants.},
  volume       = {6},
  year         = {2011},
}