Localization of SMAP2 to the TGN and its function in the regulation of TGN protein transport

Tomo Funaki; Shunsuke Kon; Roger E. Ronn; Yuji Henmi; Yuka Kobayashi; Toshio Watanabe; Keiko Nakayama; Kenji Tanabe; Masanobu Satake

doi:10.1247/csf.10022

Localization of SMAP2 to the TGN and its function in the regulation of TGN protein transport

Tomo Funaki, Shunsuke Kon, Roger E. Ronn, Yuji Henmi, Yuka Kobayashi, Toshio Watanabe, Keiko Nakayama, Kenji Tanabe, Masanobu Satake

MED - United Centers for Advanced Research and Translational Medicine (ART)

Research output: Contribution to journal › Article › peer-review

10 Citations (Scopus)

Abstract

SMAP2 is an Arf GTPase-activating protein that is located and functions on early endosome membranes. In the present study, the trans-Golgi network (TGN) was verified as an additional site of SMAP2 localization based on its co-localization with various TGN-marker proteins. Mutation of specific stretches of basic amino acid residues abolished the TGN-localization of SMAP2. Over-expression of wild-type SMAP2, but not of the mutated SMAP2, inhibited the transport of vesicular stomatitis virus-G protein from the TGN to the plasma membrane. In contrast, this transport was enhanced in SMAP2 (-/-) cells characterized by increased levels of the activated form of Arf. SMAP2 therefore belongs to an ArfGAP subtype that resides on the TGN and functions as a negative regulator of vesicle budding from the organelle.

Original language	English
Pages (from-to)	83-95
Number of pages	13
Journal	Cell Structure and Function
Volume	36
Issue number	1
DOIs	https://doi.org/10.1247/csf.10022
Publication status	Published - 2011

Keywords

Arf GTPase
Clathrin-coated vesicles
Gene targeting
Membrane traffic
Trans-Golgi network

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10.1247/csf.10022

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title = "Localization of SMAP2 to the TGN and its function in the regulation of TGN protein transport",

abstract = "SMAP2 is an Arf GTPase-activating protein that is located and functions on early endosome membranes. In the present study, the trans-Golgi network (TGN) was verified as an additional site of SMAP2 localization based on its co-localization with various TGN-marker proteins. Mutation of specific stretches of basic amino acid residues abolished the TGN-localization of SMAP2. Over-expression of wild-type SMAP2, but not of the mutated SMAP2, inhibited the transport of vesicular stomatitis virus-G protein from the TGN to the plasma membrane. In contrast, this transport was enhanced in SMAP2 (-/-) cells characterized by increased levels of the activated form of Arf. SMAP2 therefore belongs to an ArfGAP subtype that resides on the TGN and functions as a negative regulator of vesicle budding from the organelle.",

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author = "Tomo Funaki and Shunsuke Kon and Ronn, {Roger E.} and Yuji Henmi and Yuka Kobayashi and Toshio Watanabe and Keiko Nakayama and Kenji Tanabe and Masanobu Satake",

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doi = "10.1247/csf.10022",

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AU - Funaki, Tomo

AU - Kon, Shunsuke

AU - Ronn, Roger E.

AU - Henmi, Yuji

AU - Kobayashi, Yuka

AU - Watanabe, Toshio

AU - Nakayama, Keiko

AU - Tanabe, Kenji

AU - Satake, Masanobu

PY - 2011

Y1 - 2011

N2 - SMAP2 is an Arf GTPase-activating protein that is located and functions on early endosome membranes. In the present study, the trans-Golgi network (TGN) was verified as an additional site of SMAP2 localization based on its co-localization with various TGN-marker proteins. Mutation of specific stretches of basic amino acid residues abolished the TGN-localization of SMAP2. Over-expression of wild-type SMAP2, but not of the mutated SMAP2, inhibited the transport of vesicular stomatitis virus-G protein from the TGN to the plasma membrane. In contrast, this transport was enhanced in SMAP2 (-/-) cells characterized by increased levels of the activated form of Arf. SMAP2 therefore belongs to an ArfGAP subtype that resides on the TGN and functions as a negative regulator of vesicle budding from the organelle.

AB - SMAP2 is an Arf GTPase-activating protein that is located and functions on early endosome membranes. In the present study, the trans-Golgi network (TGN) was verified as an additional site of SMAP2 localization based on its co-localization with various TGN-marker proteins. Mutation of specific stretches of basic amino acid residues abolished the TGN-localization of SMAP2. Over-expression of wild-type SMAP2, but not of the mutated SMAP2, inhibited the transport of vesicular stomatitis virus-G protein from the TGN to the plasma membrane. In contrast, this transport was enhanced in SMAP2 (-/-) cells characterized by increased levels of the activated form of Arf. SMAP2 therefore belongs to an ArfGAP subtype that resides on the TGN and functions as a negative regulator of vesicle budding from the organelle.

KW - Arf GTPase

KW - Clathrin-coated vesicles

KW - Gene targeting

KW - Membrane traffic

KW - Trans-Golgi network

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SN - 0386-7196

VL - 36

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EP - 95

JO - Cell Structure and Function

JF - Cell Structure and Function

IS - 1

ER -

Localization of SMAP2 to the TGN and its function in the regulation of TGN protein transport

Abstract

Keywords

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