Structural biology of glucan phosphatases from humans to plants

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

doi:10.1016/j.sbi.2016.07.015

Structural biology of glucan phosphatases from humans to plants

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

Producción científica: Review article › revisión exhaustiva

24 Citas (Scopus)

Resumen

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.

Idioma original	English
Páginas (desde-hasta)	62-69
Número de páginas	8
Publicación	Current Opinion in Structural Biology
Volumen	40
DOI	https://doi.org/10.1016/j.sbi.2016.07.015
Estado	Published - oct 1 2016

Nota bibliográfica

Publisher Copyright:
© 2016 Elsevier Ltd

Financiación

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.

Financiadores	Número del financiador
National Science Foundation Arctic Social Science Program	IIA-1355438, MCB-1252345
National Institutes of Health (NIH)
Institute of Neurological Disorders and Stroke National Advisory Neurological Disorders and Stroke Council	R01NS070899, P01NS097197
Mizutani Foundation for Glycoscience
Kentucky Science and Engineering Foundation	KSEF-2268RDE-014, KSEF-2971-RDE-017

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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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.",

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N2 - 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.

AB - 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.

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DO - 10.1016/j.sbi.2016.07.015

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VL - 40

SP - 62

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JO - Current Opinion in Structural Biology

JF - Current Opinion in Structural Biology

ER -

Structural biology of glucan phosphatases from humans to plants

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ASJC Scopus subject areas

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