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Editorial
. 2022 Nov 30:10:1088002.
doi: 10.3389/fcell.2022.1088002. eCollection 2022.

Editorial: Unconventional protein secretion: From basic mechanisms to dysregulation in disease

Marioara Chiritoiu-Butnaru  1 , Sarah E Stewart  2 , Min Zhang  3 , Vivek Malhotra  4   5   6 , Julien Villeneuve  7
Affiliations
Editorial

Editorial: Unconventional protein secretion: From basic mechanisms to dysregulation in disease

Marioara Chiritoiu-Butnaru et al. Front Cell Dev Biol. .
No abstract available

Keywords: cell adaptation; cell compartmentalization; disease; membrane trafficking; unconventional protein secretion (UPS).

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Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

FIGURE 1
FIGURE 1
Roads and hubs of unconventional protein secretion. In addition to the conventional ER-Golgi secretory pathway, cells are endowed with additional routes for the export of cytoplasmic proteins, and multiple modes of intercellular communications have been characterized (purple). They include tunnelling nanotubes formed by membranous protrusions that emerge from the PM and connect adjacent cells. Tunnelling nanotubes allow the direct transfer of cytoplasmic proteins as well as whole organelles such as lysosomes. Outward budding of the PM produce microvesicles that are then released into the extracellular space. In types I and II UPS, cargo proteins are directly translocated across the PM by pore formation or ABC transporters, respectively. In type III UPS, cargo proteins are incorporated into intracellular compartments and transported through single or successive membrane intermediates that fuse with the PM. In type IV UPS or Golgi-bypass, integral membrane proteins are inserted into the ER and then reach the PM independently of the Golgi apparatus. Along these alternative secretory routes, cargo proteins are transported or incorporated within membrane compartments either by protein channels or by membrane remodeling defining distinct entry gates at the PM or along intracellular trafficking pathways (green). Cargo proteins can also be gathered into particular membrane intermediates prior to release into the extracellular space, defining distinct exit stations (blue). Abbreviations–αSNC: alpha-synuclein; acb1: acyl-CoA-binding protein; CFTR: cystic fibrosis transmembrane conductance regulator; CUPS: Compartment for unconventional protein secretion; CMA: Chaperone-mediated autophagy; ER: Endoplasmic reticulum; ERGIC: ER-Golgi intermediate compartment; FGF2: Fibroblast growth factor 2; Gal3: Galectin-3; IL: Interleukin; LE: Late endosome; MAPS: Misfolded-associated protein secretion; MT1-MMP: Membrane-type 1 matrix metalloproteinase; MVB: Multivesicular body; THU: TMED10-channeled UPS; UPS: Unconventional protein secretion. The figure was generating using BioRender.
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  • Editorial on the Research Topic Unconventional protein secretion: From basic mechanisms to dysregulation in disease

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