Interaction between AP-5 and the hereditary spastic paraplegia proteins SPG11 and SPG15

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Interaction between AP-5 and the hereditary spastic paraplegia proteins SPG11 and SPG15. / Hirst, Jennifer; Borner, Georg H H; Edgar, James; Hein, Marco Y; Mann, Matthias; Buchholz, Frank; Antrobus, Robin; Robinson, Margaret S.

In: Molecular Biology of the Cell, Vol. 24, No. 16, 08.2013, p. 2558-69.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Hirst, J, Borner, GHH, Edgar, J, Hein, MY, Mann, M, Buchholz, F, Antrobus, R & Robinson, MS 2013, 'Interaction between AP-5 and the hereditary spastic paraplegia proteins SPG11 and SPG15', Molecular Biology of the Cell, vol. 24, no. 16, pp. 2558-69. https://doi.org/10.1091/mbc.E13-03-0170

APA

Hirst, J., Borner, G. H. H., Edgar, J., Hein, M. Y., Mann, M., Buchholz, F., Antrobus, R., & Robinson, M. S. (2013). Interaction between AP-5 and the hereditary spastic paraplegia proteins SPG11 and SPG15. Molecular Biology of the Cell, 24(16), 2558-69. https://doi.org/10.1091/mbc.E13-03-0170

Vancouver

Hirst J, Borner GHH, Edgar J, Hein MY, Mann M, Buchholz F et al. Interaction between AP-5 and the hereditary spastic paraplegia proteins SPG11 and SPG15. Molecular Biology of the Cell. 2013 Aug;24(16):2558-69. https://doi.org/10.1091/mbc.E13-03-0170

Author

Hirst, Jennifer ; Borner, Georg H H ; Edgar, James ; Hein, Marco Y ; Mann, Matthias ; Buchholz, Frank ; Antrobus, Robin ; Robinson, Margaret S. / Interaction between AP-5 and the hereditary spastic paraplegia proteins SPG11 and SPG15. In: Molecular Biology of the Cell. 2013 ; Vol. 24, No. 16. pp. 2558-69.

Bibtex

@article{b82f07783d5245fcbddac5656db0d5f8,
title = "Interaction between AP-5 and the hereditary spastic paraplegia proteins SPG11 and SPG15",
abstract = "The AP-5 complex is a recently identified but evolutionarily ancient member of the family of heterotetrameric adaptor proteins (AP complexes). It is associated with two proteins that are mutated in patients with hereditary spastic paraplegia, SPG11 and SPG15. Here we show that the four AP-5 subunits can be coimmunoprecipitated with SPG11 and SPG15, both from cytosol and from detergent-extracted membranes, with a stoichiometry of ∼1:1:1:1:1:1. Knockdowns of SPG11 or SPG15 phenocopy knockdowns of AP-5 subunits: all six knockdowns cause the cation-independent mannose 6-phosphate receptor to become trapped in clusters of early endosomes. In addition, AP-5, SPG11, and SPG15 colocalize on a late endosomal/lysosomal compartment. Both SPG11 and SPG15 have predicted secondary structures containing α-solenoids related to those of clathrin heavy chain and COPI subunits. SPG11 also has an N-terminal, β-propeller-like domain, which interacts in vitro with AP-5. We propose that AP-5, SPG15, and SPG11 form a coat-like complex, with AP-5 involved in protein sorting, SPG15 facilitating the docking of the coat onto membranes by interacting with PI3P via its FYVE domain, and SPG11 (possibly together with SPG15) forming a scaffold.",
author = "Jennifer Hirst and Borner, {Georg H H} and James Edgar and Hein, {Marco Y} and Matthias Mann and Frank Buchholz and Robin Antrobus and Robinson, {Margaret S}",
year = "2013",
month = aug,
doi = "10.1091/mbc.E13-03-0170",
language = "English",
volume = "24",
pages = "2558--69",
journal = "Molecular Biology of the Cell",
issn = "1059-1524",
publisher = "American Society for Cell Biology",
number = "16",

}

RIS

TY - JOUR

T1 - Interaction between AP-5 and the hereditary spastic paraplegia proteins SPG11 and SPG15

AU - Hirst, Jennifer

AU - Borner, Georg H H

AU - Edgar, James

AU - Hein, Marco Y

AU - Mann, Matthias

AU - Buchholz, Frank

AU - Antrobus, Robin

AU - Robinson, Margaret S

PY - 2013/8

Y1 - 2013/8

N2 - The AP-5 complex is a recently identified but evolutionarily ancient member of the family of heterotetrameric adaptor proteins (AP complexes). It is associated with two proteins that are mutated in patients with hereditary spastic paraplegia, SPG11 and SPG15. Here we show that the four AP-5 subunits can be coimmunoprecipitated with SPG11 and SPG15, both from cytosol and from detergent-extracted membranes, with a stoichiometry of ∼1:1:1:1:1:1. Knockdowns of SPG11 or SPG15 phenocopy knockdowns of AP-5 subunits: all six knockdowns cause the cation-independent mannose 6-phosphate receptor to become trapped in clusters of early endosomes. In addition, AP-5, SPG11, and SPG15 colocalize on a late endosomal/lysosomal compartment. Both SPG11 and SPG15 have predicted secondary structures containing α-solenoids related to those of clathrin heavy chain and COPI subunits. SPG11 also has an N-terminal, β-propeller-like domain, which interacts in vitro with AP-5. We propose that AP-5, SPG15, and SPG11 form a coat-like complex, with AP-5 involved in protein sorting, SPG15 facilitating the docking of the coat onto membranes by interacting with PI3P via its FYVE domain, and SPG11 (possibly together with SPG15) forming a scaffold.

AB - The AP-5 complex is a recently identified but evolutionarily ancient member of the family of heterotetrameric adaptor proteins (AP complexes). It is associated with two proteins that are mutated in patients with hereditary spastic paraplegia, SPG11 and SPG15. Here we show that the four AP-5 subunits can be coimmunoprecipitated with SPG11 and SPG15, both from cytosol and from detergent-extracted membranes, with a stoichiometry of ∼1:1:1:1:1:1. Knockdowns of SPG11 or SPG15 phenocopy knockdowns of AP-5 subunits: all six knockdowns cause the cation-independent mannose 6-phosphate receptor to become trapped in clusters of early endosomes. In addition, AP-5, SPG11, and SPG15 colocalize on a late endosomal/lysosomal compartment. Both SPG11 and SPG15 have predicted secondary structures containing α-solenoids related to those of clathrin heavy chain and COPI subunits. SPG11 also has an N-terminal, β-propeller-like domain, which interacts in vitro with AP-5. We propose that AP-5, SPG15, and SPG11 form a coat-like complex, with AP-5 involved in protein sorting, SPG15 facilitating the docking of the coat onto membranes by interacting with PI3P via its FYVE domain, and SPG11 (possibly together with SPG15) forming a scaffold.

U2 - 10.1091/mbc.E13-03-0170

DO - 10.1091/mbc.E13-03-0170

M3 - Journal article

C2 - 23825025

VL - 24

SP - 2558

EP - 2569

JO - Molecular Biology of the Cell

JF - Molecular Biology of the Cell

SN - 1059-1524

IS - 16

ER -

ID: 88582745