Visualization of TGN to Endosome Trafficking through Fluorescently Labeled MPR and AP-1 in Living Cells
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- Satoshi Waguri
- Institut de Biologie, EP CNRS 525, Institut Pasteur de Lille, 59021 Lille Cedex, France; and
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- Frédérique Dewitte
- Institut de Biologie, EP CNRS 525, Institut Pasteur de Lille, 59021 Lille Cedex, France; and
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- Roland Le Borgne
- Institut de Biologie, EP CNRS 525, Institut Pasteur de Lille, 59021 Lille Cedex, France; and
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- Yves Rouillé
- Institut de Biologie, EP CNRS 525, Institut Pasteur de Lille, 59021 Lille Cedex, France; and
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- Yasuo Uchiyama
- Department of Cell Biology and Neuroscience (A1), Osaka University Graduate School of Medicine, Osaka, Japan
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- Jean-François Dubremetz
- Institut de Biologie, EP CNRS 525, Institut Pasteur de Lille, 59021 Lille Cedex, France; and
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- Bernard Hoflack
- Institut de Biologie, EP CNRS 525, Institut Pasteur de Lille, 59021 Lille Cedex, France; and
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- Suzanne R. Pfeffer
- editor
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<jats:p>We have stably expressed in HeLa cells a chimeric protein made of the green fluorescent protein (GFP) fused to the transmembrane and cytoplasmic domains of the mannose 6-phosphate/insulin like growth factor II receptor in order to study its dynamics in living cells. At steady state, the bulk of this chimeric protein (GFP-CI-MPR) localizes to the trans-Golgi network (TGN), but significant amounts are also detected in peripheral, tubulo-vesicular structures and early endosomes as well as at the plasma membrane. Time-lapse videomicroscopy shows that the GFP-CI-MPR is ubiquitously detected in tubular elements that detach from the TGN and move toward the cell periphery, sometimes breaking into smaller tubular fragments. The formation of the TGN-derived tubules is temperature dependent, requires the presence of intact microtubule and actin networks, and is regulated by the ARF-1 GTPase. The TGN-derived tubules fuse with peripheral, tubulo-vesicular structures also containing the GFP-CI-MPR. These structures are highly dynamic, fusing with each other as well as with early endosomes. Time-lapse videomicroscopy performed on HeLa cells coexpressing the CFP-CI-MPR and the AP-1 complex whose γ-subunit was fused to YFP shows that AP-1 is present not only on the TGN and peripheral CFP-CI-MPR containing structures but also on TGN-derived tubules containing the CFP-CI-MPR. The data support the notion that tubular elements can mediate MPR transport from the TGN to a peripheral, tubulo-vesicular network dynamically connected with the endocytic pathway and that the AP-1 coat may facilitate MPR sorting in the TGN and endosomes.</jats:p>
収録刊行物
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- Molecular Biology of the Cell
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Molecular Biology of the Cell 14 (1), 142-155, 2003-01
American Society for Cell Biology (ASCB)
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詳細情報 詳細情報について
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- CRID
- 1360574095782282240
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- NII論文ID
- 30018378390
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- NII書誌ID
- AA10830484
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- ISSN
- 19394586
- 10591524
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