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Ligand-induced structural changes of the CD44 hyaluronan-binding domain revealed by NMR.

Takeda M, Ogino S, Umemoto R, Sakakura M, Kajiwara M, Sugahara KN, Hayasaka H, Miyasaka M, Terasawa H, Shimada I
J Biol Chem 281 40089-95 (2006)
Cited: 38 times
EuropePMC logo PMID: 17085435

Abstract

CD44, a major cell surface receptor for hyaluronan (HA), contains a functional domain responsible for HA binding at its N terminus (residues 21-178). Accumulating evidence indicates that proteolytic cleavage of CD44 in its extracellular region (residues 21-268) leads to enhanced tumor cell migration and invasion. Hence, understanding the mechanisms underlying the CD44 proteolytic cleavage is important for understanding the mechanism of CD44-mediated tumor progression. Here we present the NMR structure of the HA-binding domain of CD44 in its HA-bound state. The structure is composed of the Link module (residues 32-124) and an extended lobe (residues 21-31 and 125-152). Interestingly, a comparison of its unbound and HA-bound structures revealed that rearrangement of the beta-strands in the extended lobe (residues 143-148) and disorder of the structure in the following C-terminal region (residues 153-169) occurred upon HA binding, which is consistent with the results of trypsin proteolysis studies of the CD44 HA-binding domain. The order-to-disorder transition of the C-terminal region by HA binding may be involved in the CD44-mediated cell migration.

Articles - 2i83 mentioned but not cited (9)

  1. Terminal sialic acids on CD44 N-glycans can block hyaluronan binding by forming competing intramolecular contacts with arginine sidechains. Faller CE, Guvench O. Proteins 82 3079-3089 (2014)
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  5. Zona pellucida-binding protein 2 (ZPBP2) and several proteins containing BX7B motifs in human sperm may have hyaluronic acid binding or recognition properties. Torabi F, Bogle OA, Estanyol JM, Oliva R, Miller D. Mol Hum Reprod 23 803-816 (2017)
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  8. Prediction of CD44 Structure by Deep Learning-Based Protein Modeling. Camponeschi C, Righino B, Pirolli D, Semeraro A, Ria F, De Rosa MC. Biomolecules 13 1047 (2023)
  9. Exploring the mechanism of Dahuang-Tusizi drug pair in the treatment of diabetes nephropathy based on network pharmacology and immune infiltration analysis. Liu W, Yuan L, Che M, Hou S, Meng F, Xu D, Nan Y. Medicine (Baltimore) 102 e36196 (2023)


Reviews citing this publication (9)

  1. Functional dynamics of proteins revealed by solution NMR. Osawa M, Takeuchi K, Ueda T, Nishida N, Shimada I. Curr Opin Struct Biol 22 660-669 (2012)
  2. Revealing the Mechanisms of Protein Disorder and N-Glycosylation in CD44-Hyaluronan Binding Using Molecular Simulation. Guvench O. Front Immunol 6 305 (2015)
  3. Three-dimensional structural aspects of protein-polysaccharide interactions. Nagae M, Yamaguchi Y. Int J Mol Sci 15 3768-3783 (2014)
  4. Proteolytic Processing of CD44 and Its Implications in Cancer. Medrano-González PA, Rivera-Ramírez O, Montaño LF, Rendón-Huerta EP. Stem Cells Int 2021 6667735 (2021)
  5. NMR Characterization of the Interactions Between Glycosaminoglycans and Proteins. Bu C, Jin L. Front Mol Biosci 8 646808 (2021)
  6. Functional dynamics of cell surface membrane proteins. Nishida N, Osawa M, Takeuchi K, Imai S, Stampoulis P, Kofuku Y, Ueda T, Shimada I. J Magn Reson 241 86-96 (2014)
  7. CD44 In Sarcomas: A Comprehensive Review and Future Perspectives. Fernández-Tabanera E, Melero-Fernández de Mera RM, Alonso J. Front Oncol 12 909450 (2022)
  8. Systemic Glycosaminoglycan Clearance by HARE/Stabilin-2 Activates Intracellular Signaling. Weigel PH. Cells 9 E2366 (2020)
  9. Oscillators in the microvasculature: glycocalyx and beyond. Goligorsky MS. Am J Physiol Cell Physiol 323 C432-C438 (2022)

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