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

S Hougaard; F Loechel; X Xu; R Tajima; R Albrechtsen; U M Wewer

doi:10.1006/bbrc.2000.3295

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

S Hougaard, F Loechel, X Xu, R Tajima, R Albrechtsen, U M Wewer

Department of Biomedical Sciences

52 Citations (Scopus)

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.

Original language	English
Journal	Biochemical and Biophysical Research Communications
Volume	275
Issue number	2
Pages (from-to)	261-7
Number of pages	6
ISSN	0006-291X
DOIs	https://doi.org/10.1006/bbrc.2000.3295
Publication status	Published - 2000

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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",

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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

SN - 0006-291X

VL - 275

SP - 261

EP - 267

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 2

ER -

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

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