Structural Basis for Interactions between Tenascins and Lectican C-Type Lectin Domains

Lundell, Anna; Olin, Anders I.; Mörgelin, Matthias; al-Karadaghi, Salam; Aspberg, Anders; Logan, Derek T.

doi:10.1016/j.str.2004.05.021

Cited by 127Proteoglycans and glycosaminoglycans researchGlycosylation and Glycoproteins ResearchCell Adhesion Molecules Research

Structural Basis for Interactions between Tenascins and Lectican C-Type Lectin Domains

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Lundell, Anna, Olin, Anders I., Mörgelin, Matthias, al-Karadaghi, Salam, Aspberg, Anders, Logan, Derek T.·2004·Structure

DOI 10.1016/j.str.2004.05.021

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Abstract

The C-terminal G3 domains of lecticans mediate crosslinking to diverse extracellular matrix (ECM) proteins during ECM assembly, through their C-type lectin (CLD) subdomains. The structure of the rat aggrecan CLD in a Ca(2+)-dependent complex with fibronectin type III repeats 3-5 of rat tenascin-R provides detailed support for such crosslinking. The CLD loops bind Ca2+ like other CLDs, but no carbohydrate binding is observed or possible. This is thus the first example of a direct Ca(2+)-dependent protein-protein interaction of a CLD. Surprisingly, tenascin-R does not coordinate the Ca2+ ions directly. Electron microscopy confirms that full-length tenascin-R and tenascin-C crosslink hyaluronan-aggrecan complexes. The results are significant for the binding of all lectican CLDs to tenascin-R and tenascin-C. Comparison of the protein interaction surface with that of P-selectin in complex with the PGSL-1 peptide suggests that direct protein-protein interactions of Ca(2+)-binding CLDs may be more widespread than previously appreciated.

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CSPGs like aggrecan or brevican are incorporated into perineuronal nets through their interaction with TnR and hyaluronic acid.
“Several reports suggest that CSPGs like aggrecan or brevican are incorporated into perineuronal nets through their interaction with TnR and hyaluronic acid14,53,54.”
From Elimination of the four extracellular matrix molecules tenascin-C, tenascin-R, brevican and neurocan alters the ratio of excitatory and inhibitory synapses (2019) · cites this paper as [53]
Lecticans contain binding sites for hyaluronic acid and TnR.
“Lecticans do contain binding sites for hyaluronic acid and TnR53.”
From Elimination of the four extracellular matrix molecules tenascin-C, tenascin-R, brevican and neurocan alters the ratio of excitatory and inhibitory synapses (2019) · cites this paper as [53]
Tenascin-R forms characteristic trimeric structures through association of its N-terminal domains.
“TN-R forms characteristic trimeric structures through association of their N-terminal domains.”
From The hyaluronan and proteoglycan link proteins: Organizers of the brain extracellular matrix and key molecules for neuronal function and plasticity (2015) · cites this paper as Lundell et al., 2004
The C-type lectin subdomain of lecticans binds to fibronectin type III repeats 3-5 of tenascin-R.
“The C-type lectin subdomain of lecticans binds to the fibronectin type III repeats 3-5 of TN-R, which was demonstrated by the crystal structure of the recombinant complex (Aspberg et al., 1997;Lundell et al., 2004).”
From The hyaluronan and proteoglycan link proteins: Organizers of the brain extracellular matrix and key molecules for neuronal function and plasticity (2015) · cites this paper as Lundell et al., 2004

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The Proteoglycans Aggrecan and Versican Form Networks with Fibulin-2 through Their Lectin Domain Binding
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Authors: Lundell, A., Olin, A. I., Mörgelin, M., al-Karadaghi, S., Aspberg, A., & Logan, D. T.
Affiliations: Lund University (SE)
Corresponding author: Logan, Derek T.
ORCID: Mörgelin, Matthias
Aspberg, Anders
Logan, Derek T.
Venue: Structure
Publisher: Elsevier BV
Published: 2004-08
Volume: 12
Issue: 8
Pages: 1495-1506
ISSN: 0969-2126 (ISSN-L)
DOI: 10.1016/j.str.2004.05.021
OpenAlex: W1690718176
Cited by: 127
References: 67
Citations by year: 2025: 5 · 2024: 7 · 2023: 7 · 2022: 8 · 2021: 6 · 2020: 8 · 2019: 10 · 2018: 2 · 2017: 1 · 2016: 5 · 2015: 5 · 2014: 8 · 2013: 3 · 2012: 11
FWCI: 1.39
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 3272 d)
doi.org/10.15223/policy-017 (stm-asf)
doi.org/10.15223/policy-037 (stm-asf)
doi.org/10.15223/policy-012 (stm-asf)
doi.org/10.15223/policy-029 (stm-asf)
doi.org/10.15223/policy-004 (stm-asf)
Locations: Structure (publishedVersion)
PubMed (publishedVersion)
Lund University Publications (Lund University) (submittedVersion)
Funders: Stiftelsen Konung Gustaf V:s 80-årsfond
Vetenskapsrådet
Kungliga Fysiografiska Sällskapet i Lund
Stiftelsen för Strategisk Forskning
Crafoordska Stiftelsen
Greta och Johan Kocks stiftelser
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
Keywords: tenascin-R, tenascin-C, aggrecan, fibronectin type III repeats, calcium-dependent protein-protein interaction, extracellular matrix assembly, P-selectin, protein-protein interaction surfaces
MeSH terms: Amino Acid Sequence, Animals, Calcium, Cross-Linking Reagents, Hyaluronic Acid, Models, Molecular, Molecular Sequence Data, Protein Binding, Proteoglycans, Extracellular Matrix Proteins, Sequence Homology, Amino Acid, P-Selectin, Tenascin, Lectins, C-Type, Microscopy, Electron, Transmission, Carbohydrate Metabolism, Rats, Aggrecans

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Structural Basis for Interactions between Tenascins and Lectican C-Type Lectin Domains

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