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Galectins: An Ancient Family of Carbohydrate Binding Proteins with Modern Functions

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Galectins

Part of the book series: Methods in Molecular Biology ((MIMB,volume 2442))

Abstract

Galectins are a large family of carbohydrate binding proteins with members in nearly every lineage of multicellular life. Through tandem and en-mass genome duplications, over 15 known vertebrate galectins likely evolved from a single common ancestor extant in pre-chordate lineages. While galectins have divergently evolved numerous functions, some of which do not involve carbohydrate recognition, the vast majority of the galectins have retained the conserved ability to bind variably modified polylactosamine (polyLacNAc) residues on glycans that modify proteins and lipids on the surface of host cells and pathogens. In addition to their direct role in microbial killing, many proposed galectin functions in the immune system and cancer involve crosslinking glycosylated receptors and modifying signaling pathways or sensitivity to antigen from the outside in. However, a large body of work has uncovered intracellular galectin functions mediated by carbohydrate- and non-carbohydrate-dependent interactions. In the cytoplasm, galectins can tune intracellular kinase and G-protein-coupled signaling cascades important for nutrient sensing, cell cycle progression, and transformation. Particularly, but interconnected pathways, cytoplasmic galectins serve the innate immune system as sensors of endolysosomal damage, recruiting and assembling the components of autophagosomes during intracellular infection through carbohydrate-dependent and -independent activities. In the nucleus, galectins participate in pre-mRNA splicing perhaps through interactions with non-coding RNAs required for assembly of spliceosomes. Together, studies of galectin function paint a picture of a functionally dynamic protein family recruited during eons of evolution to regulate numerous essential cellular processes in the context of multicellular life.

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Abbreviations

CBP:

Carbohydrate binding protein

CRD:

Carbohydrate recognition domain

ECM:

Extracellular matrix

ER:

Endoplasmic reticulum

GA:

Golgi apparatus

GalNAc:

N-acetylgalactosamine

GALNts:

GalNAc transferases

GBPs:

Glycan binding proteins

PNG:

Protein N glycosylation

Siglecs:

Sialic acid-binding immunoglobulin-type lectins

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Authors and Affiliations

  1. Joint Program in Transfusion Medicine, Department of Pathology, Brigham and Women’s Hospital, Harvard Medical School, Boston, MA, USA

    Hans Verkerke, Connie M. Arthur & Sean R. Stowell

  2. Harvard Glycomics Center, Harvard Medical School, Boston, MA, USA

    Hans Verkerke, Richard D. Cummings, Connie M. Arthur & Sean R. Stowell

  3. Department of Clinical Analysis, Toxicological and Bromatological, School of Pharmaceutical Sciences of Ribeirão Preto, University of São Paulo, Ribeirão Preto, Brazil

    Marcelo Dias-Baruffi

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  1. Hans Verkerke
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  2. Marcelo Dias-Baruffi
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  3. Richard D. Cummings
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  4. Connie M. Arthur
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  5. Sean R. Stowell
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Correspondence to Sean R. Stowell .

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Editors and Affiliations

  1. Joint Program in Transfusion Medicine Brigham and Women’s Hospital, Harvard Medical School, Boston, MA, USA

    Sean R. Stowell

  2. Joint Program in Transfusion Medicine Brigham and Women’s Hospital, Harvard Medical School, Boston, MA, USA

    Connie M. Arthur

  3. Department of Surgery Beth Israel Deaconess Medical Center National Center for Functional Glycomics, Harvard Medical School, Boston, MA, USA

    Richard D. Cummings

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Verkerke, H., Dias-Baruffi, M., Cummings, R.D., Arthur, C.M., Stowell, S.R. (2022). Galectins: An Ancient Family of Carbohydrate Binding Proteins with Modern Functions. In: Stowell, S.R., Arthur, C.M., Cummings, R.D. (eds) Galectins. Methods in Molecular Biology, vol 2442. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-2055-7_1

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  • DOI: https://doi.org/10.1007/978-1-0716-2055-7_1

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