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Unique carbohydrate binding platforms employed by the glucan phosphatases

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An Erratum to this article was published on 04 June 2016

Abstract

Glucan phosphatases are a family of enzymes that are functionally conserved at the enzymatic level in animals and plants. These enzymes bind and dephosphorylate glycogen in animals and starch in plants. While the enzymatic function is conserved, the glucan phosphatases employ distinct mechanisms to bind and dephosphorylate glycogen or starch. The founding member of the family is a bimodular human protein called laforin that is comprised of a carbohydrate binding module 20 (CBM20) followed by a dual specificity phosphatase domain. Plants contain two glucan phosphatases: Starch EXcess4 (SEX4) and Like Sex Four2 (LSF2). SEX4 contains a chloroplast targeting peptide, dual specificity phosphatase (DSP) domain, a CBM45, and a carboxy-terminal motif. LSF2 is comprised of simply a chloroplast targeting peptide, DSP domain, and carboxy-terminal motif. SEX4 employs an integrated DSP-CBM glucan-binding platform to engage and dephosphorylate starch. LSF2 lacks a CBM and instead utilizes two surface binding sites to bind and dephosphorylate starch. Laforin is a dimeric protein in solution and it utilizes a tetramodular architecture and cooperativity to bind and dephosphorylate glycogen. This chapter describes the biological role of glucan phosphatases in glycogen and starch metabolism and compares and contrasts their ability to bind and dephosphorylate glucans.

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Abbreviations

CBM:

Carbohydrate binding module

CGTase:

Cyclodextrin glycosyltransferase

DSP:

Dual specificity phosphatase

GWD:

Glucan-water dikinase

PWD:

Phosphoglucan-water dikinase

LSF2:

Like Sex Four2

SBS:

Surface binding site

SEX4:

Starch EXcess4

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Acknowledgments

This work was supported by National Institutes of Health Grants R01NS070899; Kentucky Science and Engineering Foundation Grants KSEF-2268RDE-014 and KSEF-2971-RDE-017; Mitzutani Foundation for Glycoscience Award; National Science Foundation Grants IIA-1355438 and MCB-1252345. M. S. G. is co-founder of OptiMol Enzymes LLC.

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    Authors and Affiliations

    1. Department of Molecular and Cellular Biochemistry and Center for Structural Biology, University of Kentucky, Lexington, KY, 40536, USA

      Shane Emanuelle, M. Kathryn Brewer & Matthew S. Gentry

    2. Division of Biology, Kansas State University, Manhattan, KS, 66506, USA

      David A. Meekins

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    1. Shane Emanuelle
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    2. M. Kathryn Brewer
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    Correspondence to Matthew S. Gentry.

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    S. Emanuelle and M. K. Brewer contributed equally to this work.

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    Emanuelle, S., Brewer, M.K., Meekins, D.A. et al. Unique carbohydrate binding platforms employed by the glucan phosphatases. Cell. Mol. Life Sci. 73, 2765–2778 (2016). https://doi.org/10.1007/s00018-016-2249-3

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