Multimeric self-assembly of autophagy initiation complexes regulated by dephosphorylation of Atg13
-
- Yamamoto Hayashi
- The University of Tokyo
Bibliographic Information
- Other Title
-
- オートファジータンパク質群の動的相互作用と分子集合形態の解析
Search this article
Description
<p>Autophagy is an intracellular recycling system conserved in eukaryotic cells. During autophagy, a part of cytoplasm is sequestered by a double-membrane structure, called the autophagosome, and transported to a lytic compartment to be degraded. At the initial step of autophagosome formation, Atg13 functions as a multipartite regulatory hub responsible for supramolecular assembly of the Atg1 complexes (composed of Atg1, Atg13, and the Atg17-Atg29-Atg31 complex); Atg13 consists of two regions, the N-terminal HORMA domain and the C-terminal intrinsically disordered region (IDR), and possesses an Atg1-binding region and two distinct Atg17-binding regions in the IDR, in which more than 40 serine residues are phosphorylated under nutrient-rich conditions. In response to starvation, these residues are dephosphorylated and Atg13 enhances the interactions with Atg1 and two molecules of Atg17, which leads to sequential assembly of the Atg1 complexes.</p>
Journal
-
- Electrophoresis Letters
-
Electrophoresis Letters 61 (2), 58-60, 2017
Japanese Electrophoresis Society
- Tweet
Keywords
Details 詳細情報について
-
- CRID
- 1390001205763371264
-
- NII Article ID
- 130006207354
-
- ISSN
- 21892636
- 21892628
-
- Text Lang
- ja
-
- Data Source
-
- JaLC
- Crossref
- CiNii Articles
-
- Abstract License Flag
- Disallowed