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MTMR4, a phosphoinositide-specific 3'-phosphatase, regulates TFEB activity and the endocytic and autophagic pathways.

フォーマット:
論文
責任表示:
Pham, Hoa Q. ; Yoshioka, Kazuaki ; Mohri, Hiromi ; Nakata, Hiroki ; Aki, Sho ; Ishimaru, Kazuhiro ; Takuwa, Noriko ; Takuwa, Yoh ; 吉岡, 和晃 ; 仲田, 浩規 ; 安藝, 翔 ; 多久和, 典子 ; 多久和, 陽
言語:
英語
出版情報:
John Wiley & Sons, 2018-08
著者名:
Pham, Hoa Q.
Yoshioka, Kazuaki
Mohri, Hiromi
Nakata, Hiroki
Aki, Sho
Ishimaru, Kazuhiro
Takuwa, Noriko
Takuwa, Yoh
吉岡, 和晃
仲田, 浩規
安藝, 翔
多久和, 典子
多久和, 陽
続きを見る
掲載情報:
Genes Cells
ISSN:
1356-9597  CiNii Research  Webcat Plus  JAIRO
巻:
23
通号:
8
開始ページ:
670
終了ページ:
687
バージョン:
author
概要:
金沢大学医薬保健研究域医学系<br />Phosphatidylinositol 3-phosphate (PI(3)P) is the predominant phosphoinositide species in early endosomes and autophagosomes, in which PI(3)P dictates traffic of these organelles. Phosphoinositide levels are tightly regulated by lipid-kinases and -phosphatases; however, a phosphatase that converts PI(3)P back to phosphatidylinositol in the endosomal and autophagosomal compartments is not fully understood. We investigated the subcellular distribution and functions of myotubularin-related protein-4 (MTMR4), which is distinct among other MTMRs in that it possesses a PI(3)P-binding FYVE domain, in lung alveolar epithelium-derived A549 cells. MTMR4 was localized mainly in late endosomes and autophagosomes. MTMR4 knockdown markedly suppressed the motility, fusion, and fission of PI(3)P-enriched structures, resulting in decreases in late endosomes, autophagosomes, and lysosomes, and enlargement of PI(3)P-enriched early and late endosomes. In amino acid- and serum-starved cells, MTMR4 knockdown decreased both autophagosomes and autolysosomes and markedly increased PI(3)P-containing autophagosomes and late endosomes, suggesting that the fusion with lysosomes of autophagosomes and late endosomes might be impaired. Notably, MTMR4 knockdown inhibited the nuclear translocation of starvation stress responsive transcription factor-EB (TFEB) with reduced expression of lysosome-related genes in starved cells. These findings indicate that MTMR4 is essential for the integrity of endocytic and autophagic pathways. © 2018 Molecular Biology Society of Japan and John Wiley & Sons Australia, Ltd.<br />Embargo Period 12 months 続きを見る
URL:
http://hdl.handle.net/2297/00053882
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