2009年4月
Distinct Transport and Intracellular Activities of Two GlcAT-P Isoforms
JOURNAL OF BIOLOGICAL CHEMISTRY
- ,
- ,
- 巻
- 284
- 号
- 14
- 開始ページ
- 9247
- 終了ページ
- 9256
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1074/jbc.M807517200
- 出版者・発行元
- AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
A neural glycotope, human natural killer-1 carbohydrate, is involved in synaptic plasticity. The key biosynthetic enzyme is a glucuronyltransferase, GlcAT-P, a type II membrane protein comprising an N-terminal cytoplasmic tail, transmembrane domain, stem region, and C-terminal catalytic domain. Previously, we reported that GlcAT-P has two isoforms differing in only the presence or absence of the N-terminal 13 amino acids (P-N13) in the cytoplasmic tail, but the functional distinction of these two isoforms has not been reported. Herein, we show that when expressed in Neuro2A cells, short form GlcAT-P (sGlcAT-P) exhibited significantly higher glucuronylation activity than the longer form (1GlcAT-P), despite their comparable specific activities in vitro. In addition, sGlcAT-P was strictly localized in Golgi apparatus, whereas lGlcAT-P was mainly localized in Golgi but partly in the endoplasmic reticulum. We demonstrated that the small GTPase, Sar1, recognized a dibasic motif in the cytoplasmic tail near P-N13 that was important for exiting the endoplasmic reticulum, and Sar1 interacted with sGlcAT-P more strongly than 1GlcAT-P. Finally, the attachment of P-N13 to another glycosyltransferase, poly-sialyltransferase-I (ST8Sia-IV), had similar effects, such as reduced activity and entrapment within endoplasmic reticulum. These results suggest that P-N13 can control glycosyltransferase transport through Sar1 binding interference.
- リンク情報
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- DOI
- https://doi.org/10.1074/jbc.M807517200
- J-GLOBAL
- https://jglobal.jst.go.jp/detail?JGLOBAL_ID=200902228983235738
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/19181664
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000264669100031&DestApp=WOS_CPL
- ID情報
-
- DOI : 10.1074/jbc.M807517200
- ISSN : 0021-9258
- eISSN : 1083-351X
- J-Global ID : 200902228983235738
- PubMed ID : 19181664
- Web of Science ID : WOS:000264669100031