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Galectins at a glance

Johannes, Ludger ; Jacob, Ralf and Leffler, Hakon LU (2018) In Journal of Cell Science 131(9).
Abstract

Galectins are carbohydrate-binding proteins that are involved in many physiological functions, such as inflammation, immune responses, cell migration, autophagy and signalling. They are also linked to diseases such as fibrosis, cancer and heart disease. How such a small family of only 15 members can have such widespread effects remains a conundrum. In this Cell Science at a Glance article, we summarise recent literature on the many cellular activities that have been ascribed to galectins. As shown on the accompanying poster, these include carbohydrate-independent interactions with cytosolic or nuclear targets and carbohydrate-dependent interactions with extracellular glycoconjugates. We discuss how these intra- and extracellular... (More)

Galectins are carbohydrate-binding proteins that are involved in many physiological functions, such as inflammation, immune responses, cell migration, autophagy and signalling. They are also linked to diseases such as fibrosis, cancer and heart disease. How such a small family of only 15 members can have such widespread effects remains a conundrum. In this Cell Science at a Glance article, we summarise recent literature on the many cellular activities that have been ascribed to galectins. As shown on the accompanying poster, these include carbohydrate-independent interactions with cytosolic or nuclear targets and carbohydrate-dependent interactions with extracellular glycoconjugates. We discuss how these intra- and extracellular activities might be linked and point out the importance of unravelling molecular mechanisms of galectin function to gain a true understanding of their contributions to the physiology of the cell. We close with a short outlook on the organismal functions of galectins and a perspective on the major challenges in the field.

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Please use this url to cite or link to this publication:
author
; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Endocytosis, Galectin, Glycosylation
in
Journal of Cell Science
volume
131
issue
9
article number
jcs208884
publisher
The Company of Biologists Ltd
external identifiers
  • scopus:85046849680
  • pmid:29717004
ISSN
0021-9533
DOI
10.1242/jcs.208884
language
English
LU publication?
yes
id
da2c9905-3c71-4afd-a2c8-ed8a1ca87df0
date added to LUP
2018-05-24 14:31:54
date last changed
2024-03-01 19:35:44
@article{da2c9905-3c71-4afd-a2c8-ed8a1ca87df0,
  abstract     = {{<p>Galectins are carbohydrate-binding proteins that are involved in many physiological functions, such as inflammation, immune responses, cell migration, autophagy and signalling. They are also linked to diseases such as fibrosis, cancer and heart disease. How such a small family of only 15 members can have such widespread effects remains a conundrum. In this Cell Science at a Glance article, we summarise recent literature on the many cellular activities that have been ascribed to galectins. As shown on the accompanying poster, these include carbohydrate-independent interactions with cytosolic or nuclear targets and carbohydrate-dependent interactions with extracellular glycoconjugates. We discuss how these intra- and extracellular activities might be linked and point out the importance of unravelling molecular mechanisms of galectin function to gain a true understanding of their contributions to the physiology of the cell. We close with a short outlook on the organismal functions of galectins and a perspective on the major challenges in the field.</p>}},
  author       = {{Johannes, Ludger and Jacob, Ralf and Leffler, Hakon}},
  issn         = {{0021-9533}},
  keywords     = {{Endocytosis; Galectin; Glycosylation}},
  language     = {{eng}},
  month        = {{05}},
  number       = {{9}},
  publisher    = {{The Company of Biologists Ltd}},
  series       = {{Journal of Cell Science}},
  title        = {{Galectins at a glance}},
  url          = {{http://dx.doi.org/10.1242/jcs.208884}},
  doi          = {{10.1242/jcs.208884}},
  volume       = {{131}},
  year         = {{2018}},
}