Dynamin-2 promotes Atg9A retrieval from phagophores during autophagy.

IF 1.8 4区 生物学 Q3 BIOLOGY
Biology Open Pub Date : 2026-10-15 Epub Date: 2026-10-16 DOI:10.1242/bio.062632
Andrew Caliri, Alejandro Martorell-Riera, Panagiota Kolitsida, Akash Saha, Cinta Iriondo-Martinez, Samuel Itskanov, Janos Steffen, Carla M Koehler, Alexander M van der Bliek
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引用次数: 0

Abstract

Autophagy involves the rapid growth of phagophores through membrane addition. This growth is triggered by vesicles containing the Atg9A protein. However, Atg9A is not incorporated into mature autophagosomes. We now demonstrate that Dynamin-2 (Dnm2) colocalizes with the BAR domain protein endophilin B1 (EndoB1/Bif-1/SH3GLB1) and other autophagy proteins when autophagy is induced. Our data suggest that Atg9A is retrieved from phagophores via fission, with help from Dnm2. Blocking Atg9A recycling, by mutating Dnm2, using RNA interference, or applying chemical inhibitors, causes Atg9A to remain in autophagosomes and be degraded during autophagy. Overall, these findings provide new insights into the roles of Dnm2 in autophagy.

在自噬过程中,Dynamin-2促进Atg9A从吞噬细胞中回收。
自噬是指通过膜的添加使吞噬细胞快速生长。这种生长是由含有Atg9A蛋白的囊泡引发的。然而,Atg9A不被纳入成熟的自噬体。我们现在证明,当自噬被诱导时,Dynamin-2 (Dnm2)与BAR结构域蛋白Endophilin-B1 (EndoB1/Bif-1/SH3GLB1)和其他自噬蛋白共定位。我们的数据表明,在Dnm2的帮助下,Atg9A通过裂变从吞噬体中回收。通过突变Dnm2、使用RNA干扰或使用化学抑制剂来阻断Atg9A循环,可导致Atg9A留在自噬体中,并在自噬过程中被降解。总的来说,这些发现为Dnm2在自噬中的作用提供了新的见解。
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来源期刊
Biology Open
Biology Open BIOLOGY-
CiteScore
3.90
自引率
0.00%
发文量
162
审稿时长
8 weeks
期刊介绍: Biology Open (BiO) is an online Open Access journal that publishes peer-reviewed original research across all aspects of the biological sciences. BiO aims to provide rapid publication for scientifically sound observations and valid conclusions, without a requirement for perceived impact.
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