Double identity: Galectins may not function as lectins inside the cell

Fu-Tong Liu

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Galectins have been shown to have a variety of activities associated with binding to extracellular glycoconjugates present on the cell surfaces and extracellular matrices. However, many galectins are detected inside the cells in locations, such as nucleus and phagosomes, suggestive of intracellular functions. In some cases, their translocation from one cellular compartment to another has been demonstrated. Specific functions consistent with intracellular localization have now been documented for some galectins. Galectin-1 and -3 have been identified as pre-mRNA splicing factors. Galectin-3, -7, and -12 have been shown to regulate apoptosis, being either anti-apoptotic or pro-apoptotic. Galectin-3 and -12 have been shown to regulate the cell cycle. The multifunctionality of these galectins is probably related to their ability to interact with multiple proteins. Indeed, a number of intracellular proteins have been identified to interact with galectins, in a manner that is dependent on protein-protein interactions, rather than lectin-carbohydrate interactions. However, their roles in the observed functions of galectins have not yet been established. Galectins have also been shown to recognize intracellular proteins through binding to their saccharide side chains. Future studies may reveal binding of galectins to glycoconjugates on internalized particles including those associated with intracellular microorganisms.

Original languageEnglish (US)
Pages (from-to)255-264
Number of pages10
JournalTrends in Glycoscience and Glycotechnology
Volume16
Issue number90
StatePublished - Jul 2004

Fingerprint

Galectins
Lectins
Galectin 3
Glycoconjugates
Proteins
Galectin 1
Phagosomes
RNA Precursors
Protein Binding
Microorganisms
Extracellular Matrix
Cell Cycle
Cells
Carbohydrates
Apoptosis

Keywords

  • Galectins
  • Glycobiology
  • Glycoconjugates
  • Intracellular protein trafficking
  • Lectin

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry

Cite this

Double identity : Galectins may not function as lectins inside the cell. / Liu, Fu-Tong.

In: Trends in Glycoscience and Glycotechnology, Vol. 16, No. 90, 07.2004, p. 255-264.

Research output: Contribution to journalArticle

@article{e278002d2d4b427ba9f2db8a59df852c,
title = "Double identity: Galectins may not function as lectins inside the cell",
abstract = "Galectins have been shown to have a variety of activities associated with binding to extracellular glycoconjugates present on the cell surfaces and extracellular matrices. However, many galectins are detected inside the cells in locations, such as nucleus and phagosomes, suggestive of intracellular functions. In some cases, their translocation from one cellular compartment to another has been demonstrated. Specific functions consistent with intracellular localization have now been documented for some galectins. Galectin-1 and -3 have been identified as pre-mRNA splicing factors. Galectin-3, -7, and -12 have been shown to regulate apoptosis, being either anti-apoptotic or pro-apoptotic. Galectin-3 and -12 have been shown to regulate the cell cycle. The multifunctionality of these galectins is probably related to their ability to interact with multiple proteins. Indeed, a number of intracellular proteins have been identified to interact with galectins, in a manner that is dependent on protein-protein interactions, rather than lectin-carbohydrate interactions. However, their roles in the observed functions of galectins have not yet been established. Galectins have also been shown to recognize intracellular proteins through binding to their saccharide side chains. Future studies may reveal binding of galectins to glycoconjugates on internalized particles including those associated with intracellular microorganisms.",
keywords = "Galectins, Glycobiology, Glycoconjugates, Intracellular protein trafficking, Lectin",
author = "Fu-Tong Liu",
year = "2004",
month = "7",
language = "English (US)",
volume = "16",
pages = "255--264",
journal = "Trends in Glycoscience and Glycotechnology",
issn = "0915-7352",
publisher = "Gakushin Publishing Company",
number = "90",

}

TY - JOUR

T1 - Double identity

T2 - Galectins may not function as lectins inside the cell

AU - Liu, Fu-Tong

PY - 2004/7

Y1 - 2004/7

N2 - Galectins have been shown to have a variety of activities associated with binding to extracellular glycoconjugates present on the cell surfaces and extracellular matrices. However, many galectins are detected inside the cells in locations, such as nucleus and phagosomes, suggestive of intracellular functions. In some cases, their translocation from one cellular compartment to another has been demonstrated. Specific functions consistent with intracellular localization have now been documented for some galectins. Galectin-1 and -3 have been identified as pre-mRNA splicing factors. Galectin-3, -7, and -12 have been shown to regulate apoptosis, being either anti-apoptotic or pro-apoptotic. Galectin-3 and -12 have been shown to regulate the cell cycle. The multifunctionality of these galectins is probably related to their ability to interact with multiple proteins. Indeed, a number of intracellular proteins have been identified to interact with galectins, in a manner that is dependent on protein-protein interactions, rather than lectin-carbohydrate interactions. However, their roles in the observed functions of galectins have not yet been established. Galectins have also been shown to recognize intracellular proteins through binding to their saccharide side chains. Future studies may reveal binding of galectins to glycoconjugates on internalized particles including those associated with intracellular microorganisms.

AB - Galectins have been shown to have a variety of activities associated with binding to extracellular glycoconjugates present on the cell surfaces and extracellular matrices. However, many galectins are detected inside the cells in locations, such as nucleus and phagosomes, suggestive of intracellular functions. In some cases, their translocation from one cellular compartment to another has been demonstrated. Specific functions consistent with intracellular localization have now been documented for some galectins. Galectin-1 and -3 have been identified as pre-mRNA splicing factors. Galectin-3, -7, and -12 have been shown to regulate apoptosis, being either anti-apoptotic or pro-apoptotic. Galectin-3 and -12 have been shown to regulate the cell cycle. The multifunctionality of these galectins is probably related to their ability to interact with multiple proteins. Indeed, a number of intracellular proteins have been identified to interact with galectins, in a manner that is dependent on protein-protein interactions, rather than lectin-carbohydrate interactions. However, their roles in the observed functions of galectins have not yet been established. Galectins have also been shown to recognize intracellular proteins through binding to their saccharide side chains. Future studies may reveal binding of galectins to glycoconjugates on internalized particles including those associated with intracellular microorganisms.

KW - Galectins

KW - Glycobiology

KW - Glycoconjugates

KW - Intracellular protein trafficking

KW - Lectin

UR - http://www.scopus.com/inward/record.url?scp=5444222746&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=5444222746&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:5444222746

VL - 16

SP - 255

EP - 264

JO - Trends in Glycoscience and Glycotechnology

JF - Trends in Glycoscience and Glycotechnology

SN - 0915-7352

IS - 90

ER -