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Review
. 2020 Aug:65:86-95.
doi: 10.1016/j.ceb.2020.02.018. Epub 2020 Apr 1.

Endosomal microdomains: Formation and function

Anne Norris  1 , Barth D Grant  2
Affiliations
Review

Endosomal microdomains: Formation and function

Anne Norris et al. Curr Opin Cell Biol. 2020 Aug.

Abstract

It is widely recognized that after endocytosis, internalized cargo is delivered to endosomes that act as sorting stations. The limiting membrane of endosomes contain specialized subregions, or microdomains, that represent distinct functions of the endosome, including regions competing for cargo capture leading to degradation or recycling. Great progress has been made in defining the endosomal protein coats that sort cargo in these domains, including Retromer that recycles transmembrane cargo, and ESCRT (endosomal sorting complex required for transport) that degrades transmembrane cargo. In this review, we discuss recent work that is beginning to unravel how such coat complexes contribute to the creation and maintenance of endosomal microdomains. We highlight data that indicates that adjacent microdomains do not act independently but rather interact to cross-regulate. We posit that these interactions provide an agile means for the cell to adjust sorting in response to extracellular signals and intracellular metabolic cues.

Keywords: Actin; Clathrin; DNAJC13; ESCRT; Endosome; HRS; ILV; Microdomain; Phospholipid; RME-8; Retromer; SNX-1; SNX1; mTORC1.

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Conflict of interest statement

Conflict of interest statement Nothing declared.

Figures

Figure 1
Figure 1
Microdomain formation by self-association and cargo interactions, with maintenance of adjacent microdomain separation by active cross-regulation. Illustration of self-associating machinery and cargo within two adjacent microdomains. Association of ESCRT-0, ubiquitinated cargo, and tetraspan proteins promotes degradative microdomain creation, whereas SNX-BAR and WASH/F-actin promote recycling microdomain formation. Ubiquitinated cargo can aid in ESCRT-0 cross-linking, and ubiquitinated tetraspan proteins can provide ubiquitin in trans for cargo that is unable to be ubiquitinated (a). Illustration of RME-8/Hsc70 anchored by SNX-BAR proteins uncoating ESCRT-0/Clathrin from the degradative microdomain at the interface of adjacent domains, helping to prevent invasion of the recycling domain by degradative machinery (b).
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