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The cancer‐associated glycosyltransferase GnT‐V (MGAT5) recognizes the N‐glycan core via residues outside its catalytic pocket.

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Title: The cancer‐associated glycosyltransferase GnT‐V (MGAT5) recognizes the N‐glycan core via residues outside its catalytic pocket.
Authors: Osuka, Reina F.1 (AUTHOR), Nagae, Masamichi2,3 (AUTHOR), Ohuchi, Akito4 (AUTHOR), Ohno, Shiho4 (AUTHOR), Yamaguchi, Yoshiki4 (AUTHOR), Kizuka, Yasuhiko1,5 (AUTHOR) kizuka.yasuhiko.k8@f.gifu-u.ac.jp
Source: FEBS Letters. Dec2023, Vol. 597 Issue 24, p3102-3113. 12p.
Subjects: Cell receptors, Molecular dynamics, Metastasis, Cell adhesion, Ligand binding (Biochemistry)
Abstract: N‐acetylglucosaminyltransferase‐V (GnT‐V or MGAT5) is a glycosyltransferase involved in cancer metastasis that creates the β1,6‐branch on N‐glycans of target proteins such as cell adhesion molecules and cell surface receptors. The 3D structure of GnT‐V and its catalytic site, which are critical for the interaction with the N‐glycan terminal, have already been revealed. However, it remains unclear how GnT‐V recognizes the core part of N‐glycan or the polypeptide part of the acceptor. Using molecular dynamics simulations and biochemical experiments, we found that several residues outside the catalytic pocket are likely involved in the recognition of the core part of N‐glycan. Furthermore, our simulation suggested that UDP binding affects the orientation of the acceptor due to the conformational change at the Manα1,6‐Man linkage. These findings provide new insights into how GnT‐V recognizes its glycoprotein substrates. [ABSTRACT FROM AUTHOR]
Copyright of FEBS Letters is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: The cancer‐associated glycosyltransferase GnT‐V (MGAT5) recognizes the N‐glycan core via residues outside its catalytic pocket.
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  Data: <searchLink fieldCode="AR" term="%22Osuka%2C+Reina+F%2E%22">Osuka, Reina F.</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Nagae%2C+Masamichi%22">Nagae, Masamichi</searchLink><relatesTo>2,3</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Ohuchi%2C+Akito%22">Ohuchi, Akito</searchLink><relatesTo>4</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Ohno%2C+Shiho%22">Ohno, Shiho</searchLink><relatesTo>4</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Yamaguchi%2C+Yoshiki%22">Yamaguchi, Yoshiki</searchLink><relatesTo>4</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Kizuka%2C+Yasuhiko%22">Kizuka, Yasuhiko</searchLink><relatesTo>1,5</relatesTo> (AUTHOR)<i> kizuka.yasuhiko.k8@f.gifu-u.ac.jp</i>
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  Data: <searchLink fieldCode="JN" term="%22FEBS+Letters%22">FEBS Letters</searchLink>. Dec2023, Vol. 597 Issue 24, p3102-3113. 12p.
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  Data: <searchLink fieldCode="DE" term="%22Cell+receptors%22">Cell receptors</searchLink><br /><searchLink fieldCode="DE" term="%22Molecular+dynamics%22">Molecular dynamics</searchLink><br /><searchLink fieldCode="DE" term="%22Metastasis%22">Metastasis</searchLink><br /><searchLink fieldCode="DE" term="%22Cell+adhesion%22">Cell adhesion</searchLink><br /><searchLink fieldCode="DE" term="%22Ligand+binding+%28Biochemistry%29%22">Ligand binding (Biochemistry)</searchLink>
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  Data: N‐acetylglucosaminyltransferase‐V (GnT‐V or MGAT5) is a glycosyltransferase involved in cancer metastasis that creates the β1,6‐branch on N‐glycans of target proteins such as cell adhesion molecules and cell surface receptors. The 3D structure of GnT‐V and its catalytic site, which are critical for the interaction with the N‐glycan terminal, have already been revealed. However, it remains unclear how GnT‐V recognizes the core part of N‐glycan or the polypeptide part of the acceptor. Using molecular dynamics simulations and biochemical experiments, we found that several residues outside the catalytic pocket are likely involved in the recognition of the core part of N‐glycan. Furthermore, our simulation suggested that UDP binding affects the orientation of the acceptor due to the conformational change at the Manα1,6‐Man linkage. These findings provide new insights into how GnT‐V recognizes its glycoprotein substrates. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of FEBS Letters is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1002/1873-3468.14775
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        Text: English
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        PageCount: 12
        StartPage: 3102
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      – SubjectFull: Cell receptors
        Type: general
      – SubjectFull: Molecular dynamics
        Type: general
      – SubjectFull: Metastasis
        Type: general
      – SubjectFull: Cell adhesion
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      – SubjectFull: Ligand binding (Biochemistry)
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      – TitleFull: The cancer‐associated glycosyltransferase GnT‐V (MGAT5) recognizes the N‐glycan core via residues outside its catalytic pocket.
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            NameFull: Osuka, Reina F.
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            NameFull: Nagae, Masamichi
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            NameFull: Ohuchi, Akito
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            NameFull: Ohno, Shiho
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            NameFull: Yamaguchi, Yoshiki
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              Text: Dec2023
              Type: published
              Y: 2023
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