The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding.

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

Standard

The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding. / Jacobsen, Linda; Madsen, Peder; Nielsen, Morten S; Geraerts, Wijnand P M; Gliemann, Jørgen; Smit, August B; Petersen, Claus M.

In: FEBS Letters, Vol. 511, No. 1-3, 2002, p. 155-8.

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

Harvard

Jacobsen, L, Madsen, P, Nielsen, MS, Geraerts, WPM, Gliemann, J, Smit, AB & Petersen, CM 2002, 'The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding.', FEBS Letters, vol. 511, no. 1-3, pp. 155-8.

APA

Jacobsen, L., Madsen, P., Nielsen, M. S., Geraerts, W. P. M., Gliemann, J., Smit, A. B., & Petersen, C. M. (2002). The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding. FEBS Letters, 511(1-3), 155-8.

Vancouver

Jacobsen L, Madsen P, Nielsen MS, Geraerts WPM, Gliemann J, Smit AB et al. The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding. FEBS Letters. 2002;511(1-3):155-8.

Author

Jacobsen, Linda ; Madsen, Peder ; Nielsen, Morten S ; Geraerts, Wijnand P M ; Gliemann, Jørgen ; Smit, August B ; Petersen, Claus M. / The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding. In: FEBS Letters. 2002 ; Vol. 511, No. 1-3. pp. 155-8.

Bibtex

@article{74cf8eb0530e11dd8d9f000ea68e967b,
title = "The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding.",
abstract = "We report that the Vps10p domain receptor sorLA binds the adaptor proteins GGA1 and -2, which take part in Golgi-endosome sorting. The GGAs bind with differential requirements via three critical residues in the C-terminal segment of the sorLA cytoplasmic tail. Unlike in sortilin and the mannose 6-phosphate receptors, the GGA-binding segment in sorLA contains neither an acidic cluster nor a dileucine. Our results support the concept of sorLA as a potential sorting receptor and suggest that key residues in sorLA and sortilin conform to a new type of motif (psi-psi-X-X-phi) defining minimum requirements for GGA binding to cytoplasmic receptor domains.",
author = "Linda Jacobsen and Peder Madsen and Nielsen, {Morten S} and Geraerts, {Wijnand P M} and J{\o}rgen Gliemann and Smit, {August B} and Petersen, {Claus M}",
note = "Keywords: ADP-Ribosylation Factors; Adaptor Proteins, Vesicular Transport; Amino Acid Sequence; Binding Sites; Carrier Proteins; Cytoplasm; Golgi Apparatus; Hydrophobicity; Methionine; Molecular Sequence Data; Protein Binding; Protein Structure, Tertiary; Proteins; Receptors, LDL; Two-Hybrid System Techniques",
year = "2002",
language = "English",
volume = "511",
pages = "155--8",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "1-3",

}

RIS

TY - JOUR

T1 - The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding.

AU - Jacobsen, Linda

AU - Madsen, Peder

AU - Nielsen, Morten S

AU - Geraerts, Wijnand P M

AU - Gliemann, Jørgen

AU - Smit, August B

AU - Petersen, Claus M

N1 - Keywords: ADP-Ribosylation Factors; Adaptor Proteins, Vesicular Transport; Amino Acid Sequence; Binding Sites; Carrier Proteins; Cytoplasm; Golgi Apparatus; Hydrophobicity; Methionine; Molecular Sequence Data; Protein Binding; Protein Structure, Tertiary; Proteins; Receptors, LDL; Two-Hybrid System Techniques

PY - 2002

Y1 - 2002

N2 - We report that the Vps10p domain receptor sorLA binds the adaptor proteins GGA1 and -2, which take part in Golgi-endosome sorting. The GGAs bind with differential requirements via three critical residues in the C-terminal segment of the sorLA cytoplasmic tail. Unlike in sortilin and the mannose 6-phosphate receptors, the GGA-binding segment in sorLA contains neither an acidic cluster nor a dileucine. Our results support the concept of sorLA as a potential sorting receptor and suggest that key residues in sorLA and sortilin conform to a new type of motif (psi-psi-X-X-phi) defining minimum requirements for GGA binding to cytoplasmic receptor domains.

AB - We report that the Vps10p domain receptor sorLA binds the adaptor proteins GGA1 and -2, which take part in Golgi-endosome sorting. The GGAs bind with differential requirements via three critical residues in the C-terminal segment of the sorLA cytoplasmic tail. Unlike in sortilin and the mannose 6-phosphate receptors, the GGA-binding segment in sorLA contains neither an acidic cluster nor a dileucine. Our results support the concept of sorLA as a potential sorting receptor and suggest that key residues in sorLA and sortilin conform to a new type of motif (psi-psi-X-X-phi) defining minimum requirements for GGA binding to cytoplasmic receptor domains.

M3 - Journal article

C2 - 11821067

VL - 511

SP - 155

EP - 158

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 1-3

ER -

ID: 5034402