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Identification of the interaction domains between α- and γ-subunits of GlcNAc-1-phosphotransferase

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Identification of the interaction domains between α- and γ-subunits of GlcNAc-1-phosphotransferase. / Velho, Renata Voltolini; De Pace, Raffaella; Tidow, Henning; Braulke, Thomas; Pohl, Sandra.

in: FEBS LETT, Jahrgang 590, Nr. 23, 12.2016, S. 4287-4295.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Velho, RV, De Pace, R, Tidow, H, Braulke, T & Pohl, S 2016, 'Identification of the interaction domains between α- and γ-subunits of GlcNAc-1-phosphotransferase', FEBS LETT, Jg. 590, Nr. 23, S. 4287-4295. https://doi.org/10.1002/1873-3468.12456

APA

Velho, R. V., De Pace, R., Tidow, H., Braulke, T., & Pohl, S. (2016). Identification of the interaction domains between α- and γ-subunits of GlcNAc-1-phosphotransferase. FEBS LETT, 590(23), 4287-4295. https://doi.org/10.1002/1873-3468.12456

Vancouver

Velho RV, De Pace R, Tidow H, Braulke T, Pohl S. Identification of the interaction domains between α- and γ-subunits of GlcNAc-1-phosphotransferase. FEBS LETT. 2016 Dez;590(23):4287-4295. https://doi.org/10.1002/1873-3468.12456

Bibtex

@article{0956ebef47ba4857899bc0f0260455c1,
title = "Identification of the interaction domains between α- and γ-subunits of GlcNAc-1-phosphotransferase",
abstract = "The disease-associated hexameric N-acetylglucosamine (GlcNAc)-1-phosphotransferase complex (α2 β2 γ2 ) catalyzes the formation of mannose 6-phosphate residues on lysosomal enzymes required for efficient targeting to lysosomes. Using pull-down experiments and mutant subunits, we identified a potential loop-like region in the α-subunits comprising residues 535-588 and 645-698 involved in the binding to γ-subunits. The interaction is independent of the mannose 6-phosphate receptor homology domain but requires the N-terminal unstructured part of the γ-subunit consisting of residues 26-69. These studies provide new insights into structural requirements for the assembly of the GlcNAc-1-phosphotransferase complex, and the functions of distinct domains of the α- and γ-subunits.",
keywords = "Acetylglucosamine, Amino Acid Sequence, Animals, HEK293 Cells, Humans, Mutation, Phenotype, Phosphotransferases, Protein Domains, Protein Subunits, Letter",
author = "Velho, {Renata Voltolini} and {De Pace}, Raffaella and Henning Tidow and Thomas Braulke and Sandra Pohl",
note = "{\textcopyright} 2016 Federation of European Biochemical Societies.",
year = "2016",
month = dec,
doi = "10.1002/1873-3468.12456",
language = "English",
volume = "590",
pages = "4287--4295",
journal = "FEBS LETT",
issn = "0014-5793",
publisher = "Elsevier",
number = "23",

}

RIS

TY - JOUR

T1 - Identification of the interaction domains between α- and γ-subunits of GlcNAc-1-phosphotransferase

AU - Velho, Renata Voltolini

AU - De Pace, Raffaella

AU - Tidow, Henning

AU - Braulke, Thomas

AU - Pohl, Sandra

N1 - © 2016 Federation of European Biochemical Societies.

PY - 2016/12

Y1 - 2016/12

N2 - The disease-associated hexameric N-acetylglucosamine (GlcNAc)-1-phosphotransferase complex (α2 β2 γ2 ) catalyzes the formation of mannose 6-phosphate residues on lysosomal enzymes required for efficient targeting to lysosomes. Using pull-down experiments and mutant subunits, we identified a potential loop-like region in the α-subunits comprising residues 535-588 and 645-698 involved in the binding to γ-subunits. The interaction is independent of the mannose 6-phosphate receptor homology domain but requires the N-terminal unstructured part of the γ-subunit consisting of residues 26-69. These studies provide new insights into structural requirements for the assembly of the GlcNAc-1-phosphotransferase complex, and the functions of distinct domains of the α- and γ-subunits.

AB - The disease-associated hexameric N-acetylglucosamine (GlcNAc)-1-phosphotransferase complex (α2 β2 γ2 ) catalyzes the formation of mannose 6-phosphate residues on lysosomal enzymes required for efficient targeting to lysosomes. Using pull-down experiments and mutant subunits, we identified a potential loop-like region in the α-subunits comprising residues 535-588 and 645-698 involved in the binding to γ-subunits. The interaction is independent of the mannose 6-phosphate receptor homology domain but requires the N-terminal unstructured part of the γ-subunit consisting of residues 26-69. These studies provide new insights into structural requirements for the assembly of the GlcNAc-1-phosphotransferase complex, and the functions of distinct domains of the α- and γ-subunits.

KW - Acetylglucosamine

KW - Amino Acid Sequence

KW - Animals

KW - HEK293 Cells

KW - Humans

KW - Mutation

KW - Phenotype

KW - Phosphotransferases

KW - Protein Domains

KW - Protein Subunits

KW - Letter

U2 - 10.1002/1873-3468.12456

DO - 10.1002/1873-3468.12456

M3 - SCORING: Journal article

C2 - 27736005

VL - 590

SP - 4287

EP - 4295

JO - FEBS LETT

JF - FEBS LETT

SN - 0014-5793

IS - 23

ER -