Trafficking of human ADAM 12-L: retention in the trans-Golgi network.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Standard

Trafficking of human ADAM 12-L: retention in the trans-Golgi network. / Hougaard, S; Loechel, F; Xu, X; Tajima, R; Albrechtsen, R; Wewer, U M.

I: Biochemical and Biophysical Research Communications, Bind 275, Nr. 2, 2000, s. 261-7.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Hougaard, S, Loechel, F, Xu, X, Tajima, R, Albrechtsen, R & Wewer, UM 2000, 'Trafficking of human ADAM 12-L: retention in the trans-Golgi network.', Biochemical and Biophysical Research Communications, bind 275, nr. 2, s. 261-7. https://doi.org/10.1006/bbrc.2000.3295

APA

Hougaard, S., Loechel, F., Xu, X., Tajima, R., Albrechtsen, R., & Wewer, U. M. (2000). Trafficking of human ADAM 12-L: retention in the trans-Golgi network. Biochemical and Biophysical Research Communications, 275(2), 261-7. https://doi.org/10.1006/bbrc.2000.3295

Vancouver

Hougaard S, Loechel F, Xu X, Tajima R, Albrechtsen R, Wewer UM. Trafficking of human ADAM 12-L: retention in the trans-Golgi network. Biochemical and Biophysical Research Communications. 2000;275(2):261-7. https://doi.org/10.1006/bbrc.2000.3295

Author

Hougaard, S ; Loechel, F ; Xu, X ; Tajima, R ; Albrechtsen, R ; Wewer, U M. / Trafficking of human ADAM 12-L: retention in the trans-Golgi network. I: Biochemical and Biophysical Research Communications. 2000 ; Bind 275, Nr. 2. s. 261-7.

Bibtex

@article{5d99b1405c7711dd8d9f000ea68e967b,
title = "Trafficking of human ADAM 12-L: retention in the trans-Golgi network.",
abstract = "We have investigated the trafficking of the membrane-anchored form of human ADAM 12 (ADAM 12-L) fused to a green fluorescence protein tag. Subcellular localization of the protein in transiently transfected cells was determined by fluorescence microscopy and trypsin sensitivity. Full-length ADAM 12-L was retained in a perinuclear compartment, which was shown to be the trans-Golgi network. In contrast, ADAM 12-L lacking the cytoplasmic domain reached the cell surface. Based on analysis of deletions and mutations of the cytoplasmic tail of ADAM 12-L, the retention signal is comprised of both the cytoplasmic and transmembrane domains, but not the Src homology 3 domain (SH3) binding sites. These results raise the possibility that a trafficking checkpoint in the trans-Golgi network is one of the cellular mechanisms for regulation of ADAM 12-L function, by allowing a rapid release of ADAM 12-L to the cell surface under specific stimuli.",
author = "S Hougaard and F Loechel and X Xu and R Tajima and R Albrechtsen and Wewer, {U M}",
note = "Keywords: ADAM Proteins; Animals; Biological Transport; CHO Cells; COS Cells; Cell Compartmentation; Cell Membrane; Cricetinae; Cytoplasm; Golgi Apparatus; Hela Cells; Humans; Immunohistochemistry; Membrane Proteins; Metalloendopeptidases; Microscopy, Fluorescence; Octoxynol",
year = "2000",
doi = "10.1006/bbrc.2000.3295",
language = "English",
volume = "275",
pages = "261--7",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Elsevier",
number = "2",

}

RIS

TY - JOUR

T1 - Trafficking of human ADAM 12-L: retention in the trans-Golgi network.

AU - Hougaard, S

AU - Loechel, F

AU - Xu, X

AU - Tajima, R

AU - Albrechtsen, R

AU - Wewer, U M

N1 - Keywords: ADAM Proteins; Animals; Biological Transport; CHO Cells; COS Cells; Cell Compartmentation; Cell Membrane; Cricetinae; Cytoplasm; Golgi Apparatus; Hela Cells; Humans; Immunohistochemistry; Membrane Proteins; Metalloendopeptidases; Microscopy, Fluorescence; Octoxynol

PY - 2000

Y1 - 2000

N2 - We have investigated the trafficking of the membrane-anchored form of human ADAM 12 (ADAM 12-L) fused to a green fluorescence protein tag. Subcellular localization of the protein in transiently transfected cells was determined by fluorescence microscopy and trypsin sensitivity. Full-length ADAM 12-L was retained in a perinuclear compartment, which was shown to be the trans-Golgi network. In contrast, ADAM 12-L lacking the cytoplasmic domain reached the cell surface. Based on analysis of deletions and mutations of the cytoplasmic tail of ADAM 12-L, the retention signal is comprised of both the cytoplasmic and transmembrane domains, but not the Src homology 3 domain (SH3) binding sites. These results raise the possibility that a trafficking checkpoint in the trans-Golgi network is one of the cellular mechanisms for regulation of ADAM 12-L function, by allowing a rapid release of ADAM 12-L to the cell surface under specific stimuli.

AB - We have investigated the trafficking of the membrane-anchored form of human ADAM 12 (ADAM 12-L) fused to a green fluorescence protein tag. Subcellular localization of the protein in transiently transfected cells was determined by fluorescence microscopy and trypsin sensitivity. Full-length ADAM 12-L was retained in a perinuclear compartment, which was shown to be the trans-Golgi network. In contrast, ADAM 12-L lacking the cytoplasmic domain reached the cell surface. Based on analysis of deletions and mutations of the cytoplasmic tail of ADAM 12-L, the retention signal is comprised of both the cytoplasmic and transmembrane domains, but not the Src homology 3 domain (SH3) binding sites. These results raise the possibility that a trafficking checkpoint in the trans-Golgi network is one of the cellular mechanisms for regulation of ADAM 12-L function, by allowing a rapid release of ADAM 12-L to the cell surface under specific stimuli.

U2 - 10.1006/bbrc.2000.3295

DO - 10.1006/bbrc.2000.3295

M3 - Journal article

C2 - 10964655

VL - 275

SP - 261

EP - 267

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 2

ER -

ID: 5236450