Direct link between Atg protein and small GTPase Rab: Atg16L functions as a potential Rab33 effector in mammals

Mitsunori Fukuda, Takashi Itoh

研究成果: ジャーナルへの寄稿学術論文査読

42 被引用数 (Scopus)

抄録

Atg16L is a factor that is essential for elongation of the isolation membrane (also called phagophore), a precursor of the autophagosome. Atg16L facilitates LC3/Atg8-conjugation to phosphatidylethanolamine by forming an oligomeric complex with Atg12-conjugated Atg5 and recruiting an LC3-Atg3 intermediate to elongating isolation membranes. Although Atg16L is responsible for the isolation membrane localization of the complex, the mechanism by which Atg16L is targeted to or recognizes isolation membranes remains largely unknown. We recently reported finding that Atg16L specifically and directly interacts with the Golgi-resident small GTPase Rab33B (and Rab33A) via the coiled-coil domain of Atg16L. Since expression of a GTPase-deficient mutant of Rab33B or the coiled-coil domain of Atg16L modulates macroautophagy (simply referred to as autophagy below), Atg16L (or the Atg12-5/16L complex) is likely to function as a specific effector molecule for Rab33 in autophagosome formation. Future study of the cross talk between Atg16L-mediated autophagosome formation and Rab33-mediated membrane trafficking should provide an important clue to unresolved issues in autophagosome formation, specifically, the membrane source of autophagosomes.

本文言語英語
ページ(範囲)824-826
ページ数3
ジャーナルAutophagy
4
6
DOI
出版ステータス出版済み - 2008 8月 16

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