IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v9y2018i1d10.1038_s41467-018-05825-x.html
   My bibliography  Save this article

Insights into degradation mechanism of N-end rule substrates by p62/SQSTM1 autophagy adapter

Author

Listed:
  • Do Hoon Kwon

    (Korea University)

  • Ok Hyun Park

    (Korea University
    Korea University)

  • Leehyeon Kim

    (Korea University)

  • Yang Ouk Jung

    (Korea University)

  • Yeonkyoung Park

    (Korea University
    Korea University)

  • Hyeongseop Jeong

    (Korea Basic Science Institute)

  • Jaekyung Hyun

    (Korea Basic Science Institute)

  • Yoon Ki Kim

    (Korea University
    Korea University)

  • Hyun Kyu Song

    (Korea University)

Abstract

p62/SQSTM1 is the key autophagy adapter protein and the hub of multi-cellular signaling. It was recently reported that autophagy and N-end rule pathways are linked via p62. However, the exact recognition mode of degrading substrates and regulation of p62 in the autophagic pathway remain unknown. Here, we present the complex structures between the ZZ-domain of p62 and various type-1 and type-2 N-degrons. The binding mode employed in the interaction of the ZZ-domain with N-degrons differs from that employed by classic N-recognins. It was also determined that oligomerization via the PB1 domain can control functional affinity to the R-BiP substrate. Unexpectedly, we found that self-oligomerization and disassembly of p62 are pH-dependent. These findings broaden our understanding of the functional repertoire of the N-end rule pathway and provide an insight into the regulation of p62 during the autophagic pathway.

Suggested Citation

  • Do Hoon Kwon & Ok Hyun Park & Leehyeon Kim & Yang Ouk Jung & Yeonkyoung Park & Hyeongseop Jeong & Jaekyung Hyun & Yoon Ki Kim & Hyun Kyu Song, 2018. "Insights into degradation mechanism of N-end rule substrates by p62/SQSTM1 autophagy adapter," Nature Communications, Nature, vol. 9(1), pages 1-13, December.
  • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-05825-x
    DOI: 10.1038/s41467-018-05825-x
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-018-05825-x
    File Function: Abstract
    Download Restriction: no

    File URL: https://libkey.io/10.1038/s41467-018-05825-x?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Jianxiu Zhang & Ying-Ying Wang & Zhao-Qian Pan & Yulu Li & Jianhua Sui & Li-Lin Du & Keqiong Ye, 2022. "Structural mechanism of protein recognition by the FW domain of autophagy receptor Nbr1," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    2. Pureum Jeon & Hyun-Ji Ham & Haneul Choi & Semin Park & Jae-Woo Jang & Sang-Won Park & Dong-Hyung Cho & Hyun-Jeong Lee & Hyun Kyu Song & Masaaki Komatsu & Dohyun Han & Deok-Jin Jang & Jin-A Lee, 2024. "NS1 binding protein regulates stress granule dynamics and clearance by inhibiting p62 ubiquitination," Nature Communications, Nature, vol. 15(1), pages 1-16, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-05825-x. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.