Hanging the coat on a collar: Same function but different localization and mechanism for COPII

Yehonathan Malis, Koret Hirschberg, Christoph Kaether

Research output: Contribution to journalArticlepeer-review

Abstract

An entirely different mechanism and localization were recently proposed for the COPII coat complex, challenging its well-accepted function to select and concentrate cargo into small COPII-coated spherical transport vesicles. Instead, the COPII complex is suggested to form a dynamic yet stationary collar that forms a boundary between the ER and the ER export membrane domain. This membrane domain, the ER exit site (ERES), is the site of COPII-mediated sorting and concentration of transport competent proteins. Subsequently, the ERES is implicated to mature and bud to form a sizeable pleiomorphic transport carrier that translocate on microtubules to fuse with the Golgi apparatus. Despite this drastic mechanistic dogma shift, most of the underlying protein-protein and protein-membrane interactions remain unchanged. Here, we attempt to provide a detailed description of the newly proposed model of how ER to Golgi transport works by describing the role of several essential proteins of the transport machinery.

Original languageEnglish
Article number2200064
JournalBioEssays
Volume44
Issue number10
DOIs
StatePublished - Oct 2022

Keywords

  • COPII
  • ER exit site
  • cargo protein
  • early secretory pathway
  • endoplasmic reticulum
  • transport carriers
  • transport vesicles

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