Research ExplorerPublicationsFunctional organization of the sortilin Vps10p domain.

Functional organization of the sortilin Vps10p domain.

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Functional organization of the sortilin Vps10p domain. / Westergaard, Uffe B; Sørensen, Esben S; Hermey, Guido; Nielsen, Morten S; Nykjaer, Anders; Kirkegaard, Kirstine; Jacobsen, Christian; Gliemann, Jørgen; Madsen, Peder; Petersen, Claus Munck.

In: J BIOL CHEM, Vol. 279, No. 48, 48, 2004, p. 50221-50229.

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

Harvard

Westergaard, UB, Sørensen, ES, Hermey, G, Nielsen, MS, Nykjaer, A, Kirkegaard, K, Jacobsen, C, Gliemann, J, Madsen, P & Petersen, CM 2004, 'Functional organization of the sortilin Vps10p domain.', J BIOL CHEM, vol. 279, no. 48, 48, pp. 50221-50229. <http://www.ncbi.nlm.nih.gov/pubmed/15364913?dopt=Citation>

APA

Westergaard, U. B., Sørensen, E. S., Hermey, G., Nielsen, M. S., Nykjaer, A., Kirkegaard, K., Jacobsen, C., Gliemann, J., Madsen, P., & Petersen, C. M. (2004). Functional organization of the sortilin Vps10p domain. J BIOL CHEM, 279(48), 50221-50229. [48]. http://www.ncbi.nlm.nih.gov/pubmed/15364913?dopt=Citation

Vancouver

Westergaard UB, Sørensen ES, Hermey G, Nielsen MS, Nykjaer A, Kirkegaard K et al. Functional organization of the sortilin Vps10p domain. J BIOL CHEM. 2004;279(48):50221-50229. 48.

Bibtex

@article{f30da1b52fae4c5baa847851968e3e19,
title = "Functional organization of the sortilin Vps10p domain.",
abstract = "A Vps10p domain makes up the entire luminal part of Sortilin, and this type of domain is the hallmark of a new family of neuronal receptors that target a variety of ligands, including neurotrophins and neuropeptides. We have shown that two structural features of the Vps10p domain, the N-terminal propeptide and the C-terminal segment of ten conserved cysteines (10CC), are key elements in the function of Sortilin. The propeptide has two functions. (i) It binds the mature part of Sortilin and prevents ligands in the biosynthetic pathway from binding to the uncleaved proreceptor, and (ii) it facilitates receptor transport in early Golgi compartments by a mechanism that does not depend on its ability to prevent ligand binding. In contrast, other Vps10p domain receptors, such as SorLA and SorCS3, do not need their propeptide for normal and swift processing. The 10CC segment constitutes an exchangeable module containing five conserved disulfide bridges, and using module-shuffling and truncations, we have shown that the 10CC segment is a major ligand-binding region in Sortilin.",
author = "Westergaard, {Uffe B} and S{\o}rensen, {Esben S} and Guido Hermey and Nielsen, {Morten S} and Anders Nykjaer and Kirstine Kirkegaard and Christian Jacobsen and J{\o}rgen Gliemann and Peder Madsen and Petersen, {Claus Munck}",
year = "2004",
language = "Deutsch",
volume = "279",
pages = "50221--50229",
journal = "J BIOL CHEM",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "48",

}

RIS

TY - JOUR

T1 - Functional organization of the sortilin Vps10p domain.

AU - Westergaard, Uffe B

AU - Sørensen, Esben S

AU - Hermey, Guido

AU - Nielsen, Morten S

AU - Nykjaer, Anders

AU - Kirkegaard, Kirstine

AU - Jacobsen, Christian

AU - Gliemann, Jørgen

AU - Madsen, Peder

AU - Petersen, Claus Munck

PY - 2004

Y1 - 2004

N2 - A Vps10p domain makes up the entire luminal part of Sortilin, and this type of domain is the hallmark of a new family of neuronal receptors that target a variety of ligands, including neurotrophins and neuropeptides. We have shown that two structural features of the Vps10p domain, the N-terminal propeptide and the C-terminal segment of ten conserved cysteines (10CC), are key elements in the function of Sortilin. The propeptide has two functions. (i) It binds the mature part of Sortilin and prevents ligands in the biosynthetic pathway from binding to the uncleaved proreceptor, and (ii) it facilitates receptor transport in early Golgi compartments by a mechanism that does not depend on its ability to prevent ligand binding. In contrast, other Vps10p domain receptors, such as SorLA and SorCS3, do not need their propeptide for normal and swift processing. The 10CC segment constitutes an exchangeable module containing five conserved disulfide bridges, and using module-shuffling and truncations, we have shown that the 10CC segment is a major ligand-binding region in Sortilin.

AB - A Vps10p domain makes up the entire luminal part of Sortilin, and this type of domain is the hallmark of a new family of neuronal receptors that target a variety of ligands, including neurotrophins and neuropeptides. We have shown that two structural features of the Vps10p domain, the N-terminal propeptide and the C-terminal segment of ten conserved cysteines (10CC), are key elements in the function of Sortilin. The propeptide has two functions. (i) It binds the mature part of Sortilin and prevents ligands in the biosynthetic pathway from binding to the uncleaved proreceptor, and (ii) it facilitates receptor transport in early Golgi compartments by a mechanism that does not depend on its ability to prevent ligand binding. In contrast, other Vps10p domain receptors, such as SorLA and SorCS3, do not need their propeptide for normal and swift processing. The 10CC segment constitutes an exchangeable module containing five conserved disulfide bridges, and using module-shuffling and truncations, we have shown that the 10CC segment is a major ligand-binding region in Sortilin.

M3 - SCORING: Zeitschriftenaufsatz

VL - 279

SP - 50221

EP - 50229

JO - J BIOL CHEM

JF - J BIOL CHEM

SN - 0021-9258

IS - 48

M1 - 48

ER -