Abstract
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 language | English |
|---|---|
| Pages (from-to) | 62-69 |
| Number of pages | 8 |
| Journal | Current Opinion in Structural Biology |
| Volume | 40 |
| DOIs | |
| State | Published - 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