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Rer1p, a retrieval receptor for endoplasmic reticulum membrane proteins, is dynamically localized to the Golgi apparatus by coatomer.

Sato K, Sato M, Nakano A - J. Cell Biol. (2001)

Bottom Line: Either a lesion of coatomer or deletion of the COOH-terminal tail of Rer1p causes its mislocalization to the vacuole.The COOH-terminal Rer1p tail interacts in vitro with a coatomer complex containing alpha and gamma subunits.These findings not only give the proof that Rer1p is a novel type of retrieval receptor recognizing the TMD in the Golgi but also indicate that coatomer actively regulates the function and localization of Rer1p.

View Article: PubMed Central - PubMed

Affiliation: Molecular Membrane Biology Laboratory, RIKEN (The Institute of Physical and Chemical Research), Saitama 351-0198, Japan. satoken@postman.riken.go.jp

ABSTRACT
Rer1p, a yeast Golgi membrane protein, is required for the retrieval of a set of endoplasmic reticulum (ER) membrane proteins. We present the first evidence that Rer1p directly interacts with the transmembrane domain (TMD) of Sec12p which contains a retrieval signal. A green fluorescent protein (GFP) fusion of Rer1p rapidly cycles between the Golgi and the ER. Either a lesion of coatomer or deletion of the COOH-terminal tail of Rer1p causes its mislocalization to the vacuole. The COOH-terminal Rer1p tail interacts in vitro with a coatomer complex containing alpha and gamma subunits. These findings not only give the proof that Rer1p is a novel type of retrieval receptor recognizing the TMD in the Golgi but also indicate that coatomer actively regulates the function and localization of Rer1p.

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Real-time movements of GFP-Rer1p and GFP-Rer1Δ25p in living cells. Wild-type cells expressing GFP-Rer1p (A–C) and Δpep4 cells expressing GFP-Rer1Δ25p (D–F) were grown to the early log phase at 20°C, and images were collected by real-time confocal fluorescence microscopy. Frames are taken at the indicated times (in seconds). Videos are available at http://www.jcb.org/cgi/content/full/152/5/935/DC1.
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Figure 2: Real-time movements of GFP-Rer1p and GFP-Rer1Δ25p in living cells. Wild-type cells expressing GFP-Rer1p (A–C) and Δpep4 cells expressing GFP-Rer1Δ25p (D–F) were grown to the early log phase at 20°C, and images were collected by real-time confocal fluorescence microscopy. Frames are taken at the indicated times (in seconds). Videos are available at http://www.jcb.org/cgi/content/full/152/5/935/DC1.

Mentions: Video 1 and 2 (available at http://www.jcb.org/cgi/content/full/152/5/935/DC1) further depict Fig. 2. Images of wild-type cells expressing GFP-Rer1p (Video 1) and Δpep4 cells expressing GFP-Rer1Δ25p (Video 2) were captured at the video rate (30 frames/s) by an Olympus BX-60 fluorescence microscope equipped with a confocal laser scanner unit CSU10 in combination with an image intensifier (VS4-1845; Video Scope) and a high-speed CCD camera (CCD-300T-RC; Dage-MTI) and processed by the IPLab software (Scanalytics).


Rer1p, a retrieval receptor for endoplasmic reticulum membrane proteins, is dynamically localized to the Golgi apparatus by coatomer.

Sato K, Sato M, Nakano A - J. Cell Biol. (2001)

Real-time movements of GFP-Rer1p and GFP-Rer1Δ25p in living cells. Wild-type cells expressing GFP-Rer1p (A–C) and Δpep4 cells expressing GFP-Rer1Δ25p (D–F) were grown to the early log phase at 20°C, and images were collected by real-time confocal fluorescence microscopy. Frames are taken at the indicated times (in seconds). Videos are available at http://www.jcb.org/cgi/content/full/152/5/935/DC1.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2198819&req=5

Figure 2: Real-time movements of GFP-Rer1p and GFP-Rer1Δ25p in living cells. Wild-type cells expressing GFP-Rer1p (A–C) and Δpep4 cells expressing GFP-Rer1Δ25p (D–F) were grown to the early log phase at 20°C, and images were collected by real-time confocal fluorescence microscopy. Frames are taken at the indicated times (in seconds). Videos are available at http://www.jcb.org/cgi/content/full/152/5/935/DC1.
Mentions: Video 1 and 2 (available at http://www.jcb.org/cgi/content/full/152/5/935/DC1) further depict Fig. 2. Images of wild-type cells expressing GFP-Rer1p (Video 1) and Δpep4 cells expressing GFP-Rer1Δ25p (Video 2) were captured at the video rate (30 frames/s) by an Olympus BX-60 fluorescence microscope equipped with a confocal laser scanner unit CSU10 in combination with an image intensifier (VS4-1845; Video Scope) and a high-speed CCD camera (CCD-300T-RC; Dage-MTI) and processed by the IPLab software (Scanalytics).

Bottom Line: Either a lesion of coatomer or deletion of the COOH-terminal tail of Rer1p causes its mislocalization to the vacuole.The COOH-terminal Rer1p tail interacts in vitro with a coatomer complex containing alpha and gamma subunits.These findings not only give the proof that Rer1p is a novel type of retrieval receptor recognizing the TMD in the Golgi but also indicate that coatomer actively regulates the function and localization of Rer1p.

View Article: PubMed Central - PubMed

Affiliation: Molecular Membrane Biology Laboratory, RIKEN (The Institute of Physical and Chemical Research), Saitama 351-0198, Japan. satoken@postman.riken.go.jp

ABSTRACT
Rer1p, a yeast Golgi membrane protein, is required for the retrieval of a set of endoplasmic reticulum (ER) membrane proteins. We present the first evidence that Rer1p directly interacts with the transmembrane domain (TMD) of Sec12p which contains a retrieval signal. A green fluorescent protein (GFP) fusion of Rer1p rapidly cycles between the Golgi and the ER. Either a lesion of coatomer or deletion of the COOH-terminal tail of Rer1p causes its mislocalization to the vacuole. The COOH-terminal Rer1p tail interacts in vitro with a coatomer complex containing alpha and gamma subunits. These findings not only give the proof that Rer1p is a novel type of retrieval receptor recognizing the TMD in the Golgi but also indicate that coatomer actively regulates the function and localization of Rer1p.

Show MeSH