Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2024 Jul 11;46(1-2):4.
doi: 10.1007/s00281-024-01010-z.

Intracellular galectin interactions in health and disease

Ralf Jacob  1 , Lena-Sophie Gorek  2
Affiliations
Review

Intracellular galectin interactions in health and disease

Ralf Jacob et al. Semin Immunopathol. .

Abstract

In the galectin family, a group of lectins is united by their evolutionarily conserved carbohydrate recognition domains. These polypeptides play a role in various cellular processes and are implicated in disease mechanisms such as cancer, fibrosis, infection, and inflammation. Following synthesis in the cytosol, manifold interactions of galectins have been described both extracellularly and intracellularly. Extracellular galectins frequently engage with glycoproteins or glycolipids in a carbohydrate-dependent manner. Intracellularly, galectins bind to non-glycosylated proteins situated in distinct cellular compartments, each with multiple cellular functions. This diversity complicates attempts to form a comprehensive understanding of the role of galectin molecules within the cell. This review enumerates intracellular galectin interaction partners and outlines their involvement in cellular processes. The intricate connections between galectin functions and pathomechanisms are illustrated through discussions of intracellular galectin assemblies in immune and cancer cells. This underscores the imperative need to fully comprehend the interplay of galectins with the cellular machinery and to devise therapeutic strategies aimed at counteracting the establishment of galectin-based disease mechanisms.

Keywords: Cancer; Galectin; Immune cell; Protein interaction.

PubMed Disclaimer

Conflict of interest statement

The authors have no relevant financial or non-financial interests to disclose.

Figures

Fig. 1
Fig. 1
Domain structure of galectin subtypes. Prototype galectins contain one CRD, galectin-1, -2, -5, -7, -10, -11, -13, -14 and − 16. They are often characterized by a dimeric quaternary structure. Tandem repeat-type galectin-4, -6, -8, -9 and 12 are characterized by two CRDs. The only chimera-type galectin with a dynamic proline/tyrosine/glycine-repeat N-terminal domain and one C-terminal CRD is galectin-3. Type-C and Type-N-self-association by the C- or N-terminal domain into oligomeric assemblies have been described
Fig. 2
Fig. 2
Intracellular binding partners of galectins in distinct cellular processes. Different cellular localizations and interaction partners of galectins are exemplified on a scheme depicting cellular organelles. Subtypes of prototype and tandem repeat galectins are indicated. E, endosome; LT, lactotransferrin; MVE, multivesicular endosome; SE, sorting endosome; V, transport vesicle
See this image and copyright information in PMC

Similar articles

See all similar articles

References

    1. Reily C, Stewart TJ, Renfrow MB, Novak J (2019) Glycosylation in health and disease. Nat Rev Nephrol 15(6):346–366. 10.1038/s41581-019-0129-4 10.1038/s41581-019-0129-4 - DOI - PMC - PubMed
    1. Barondes SH, Cooper DN, Gitt MA, Leffler H (1994) Galectins. Structure and function of a large family of animal lectins. JBiolChem 269(33):20807–20810 - PubMed
    1. Teichberg VI, Silman I, Beitsch DD, Resheff G (1975) A beta-D-galactoside binding protein from electric organ tissue of Electrophorus electricus. Proc Natl Acad Sci USA 72(4):1383–1387. 10.1073/pnas.72.4.1383 10.1073/pnas.72.4.1383 - DOI - PMC - PubMed
    1. Lobsanov YD, Gitt MA, Leffler H, Barondes SH, Rini JM (1993) X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution. J Biol Chem 268(36):27034–27038. 10.2210/pdb1hlc/pdb 10.2210/pdb1hlc/pdb - DOI - PubMed
    1. Houzelstein D, Goncalves IR, Fadden AJ, Sidhu SS, Cooper DN, Drickamer K, Leffler H, Poirier F (2004) Phylogenetic analysis of the vertebrate galectin family. Mol Biol Evol 21(7):1177–1187. 10.1093/molbev/msh082 10.1093/molbev/msh082 - DOI - PubMed

LinkOut - more resources