Structural biology of glucan phosphatases from humans to plants

Matthew S. Gentry, M. Kathryn Brewer, Craig W. Vander Kooi

Research output: Contribution to journalReview articlepeer-review

17 Scopus citations


Glucan phosphatases are functionally conserved at the enzymatic level, dephosphorylating glycogen in animals and starch in plants. The human glucan phosphatase laforin is the founding member of the family and it is comprised of a carbohydrate binding module (CBM) domain followed by a dual specificity phosphatase (DSP) domain. Plants encode two glucan phosphatases: Starch EXcess4 (SEX4) and Like Sex Four2 (LSF2). SEX4 contains a DSP domain followed by a CBM domain, while LSF2 contains a DSP domain and lacks a CBM. This review demonstrates how glucan phosphatase function is conserved and highlights how each family member employs a unique mechanism to bind and dephosphorylate glucan substrates.

Original languageEnglish
Pages (from-to)62-69
Number of pages8
JournalCurrent Opinion in Structural Biology
StatePublished - Oct 1 2016

Bibliographical note

Funding Information:
Research reported in this publication was supported by the National Institute of Neurological Disorders And Stroke of the National Institutes of Health under Award Numbers R01NS070899 and P01NS097197 , Kentucky Science and Engineering Foundation grants KSEF-2268RDE-014 and KSEF-2971-RDE-017 , a Mitzutani Foundation for Glycoscience award, and National Science Foundation grants IIA-1355438 and MCB-1252345 . The content is solely the responsibility of the authors and does not necessarily represent the official views of the funding agencies.

Publisher Copyright:
© 2016 Elsevier Ltd

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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