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Related Experiment Video

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Complementation of Splicing Activity by a Galectin-3 - U1 snRNP Complex on Beads
08:48

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Published on: December 9, 2020

Galectin multimerization and lattice formation are regulated by linker region structure.

Lesley A Earl1, Shuguang Bi, Linda G Baum

  • 1Department of Pathology and Laboratory Medicine, UCLA School of Medicine, Los Angeles, CA 90095, USA.

Glycobiology
|September 25, 2010
PubMed
Summary

Tandem-repeat galectins are more potent cell death inducers than prototype galectins. Their linker domains enable multimer formation, enhancing glycan binding and T cell death signaling.

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Last Updated: Jun 8, 2026

Complementation of Splicing Activity by a Galectin-3 - U1 snRNP Complex on Beads
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Published on: September 28, 2020

Area of Science:

  • Glycobiology
  • Immunology
  • Molecular Cell Biology

Background:

  • Galectins are proteins that bind to carbohydrates (glycans) on cell surfaces, regulating cellular functions.
  • Prototype galectins (e.g., galectin-1) have one carbohydrate recognition domain (CRD) and dimerize, while tandem-repeat galectins (e.g., galectin-9) have two CRDs linked together.
  • Both CRDs in tandem-repeat galectins, or dimerized CRDs in prototype galectins, are crucial for crosslinking cell surface receptors and initiating cell signaling.

Purpose of the Study:

  • To investigate why tandem-repeat galectins are more potent than prototype galectins in inducing cell death.
  • To determine if the linker domain, rather than CRD specificity, accounts for the increased potency of tandem-repeat galectins.
  • To elucidate the structural basis for enhanced galectin function.

Main Methods:

  • Engineered three tandem-repeat galectin constructs using identical galectin-1 CRDs but varying linker regions.
  • Assessed the impact of different linker types (random-coil, rigid α-helical, short rigid) on galectin structure and function.
  • Quantified galectin binding to glycan ligands and cell surface glycoprotein receptors.
  • Measured the induction of T cell death by the engineered galectin constructs.

Main Results:

  • Linker regions that allowed for separation of the two galectin-1 CRDs (random-coil or rigid α-helical) promoted the formation of higher-order galectin multimers.
  • These higher-order multimers exhibited enhanced binding to glycan ligands and cell surface glycoprotein receptors.
  • Galectin constructs with flexible linkers were significantly more potent in triggering T cell death compared to native galectin-1 or constructs with short, rigid linkers.

Conclusions:

  • The increased potency of tandem-repeat galectins in inducing cell death is primarily attributed to the linker domain.
  • The linker facilitates intermolecular CRD interactions, leading to the formation of higher-order, multivalent galectin structures.
  • These higher-order multimers exhibit enhanced biological activity, including more effective induction of T cell death, independent of CRD specificity.