Selective Secretion of KDEL-Bearing Proteins: Mechanisms and Functions

In multicellular organisms, cells must continuously exchange messages with the right meaning, intensity, and duration. Most of these messages are delivered through cognate interactions between membrane and secretory proteins. Their conformational maturation is assisted by a vast array of chaperones...

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Main Authors: F. C. Palazzo, R. Sitia, T. Tempio
Format: Article
Language:English
Published: Frontiers Media S.A. 2022-07-01
Series:Frontiers in Cell and Developmental Biology
Subjects:
Online Access:https://www.frontiersin.org/articles/10.3389/fcell.2022.967875/full
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author F. C. Palazzo
R. Sitia
T. Tempio
author_facet F. C. Palazzo
R. Sitia
T. Tempio
author_sort F. C. Palazzo
collection DOAJ
description In multicellular organisms, cells must continuously exchange messages with the right meaning, intensity, and duration. Most of these messages are delivered through cognate interactions between membrane and secretory proteins. Their conformational maturation is assisted by a vast array of chaperones and enzymes, ensuring the fidelity of intercellular communication. These folding assistants reside in the early secretory compartment (ESC), a functional unit that encompasses endoplasmic reticulum (ER), intermediate compartment and cis-Golgi. Most soluble ESC residents have C-terminal KDEL-like motifs that prevent their transport beyond the Golgi. However, some accumulate in the ER, while others in downstream stations, implying different recycling rates. Moreover, it is now clear that cells can actively secrete certain ESC residents but not others. This essay discusses the physiology of their differential intracellular distribution, and the mechanisms that may ensure selectivity of release.
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spelling doaj.art-026accd2574546e2bcf3b0a0d0f621002022-12-22T03:01:53ZengFrontiers Media S.A.Frontiers in Cell and Developmental Biology2296-634X2022-07-011010.3389/fcell.2022.967875967875Selective Secretion of KDEL-Bearing Proteins: Mechanisms and FunctionsF. C. PalazzoR. SitiaT. TempioIn multicellular organisms, cells must continuously exchange messages with the right meaning, intensity, and duration. Most of these messages are delivered through cognate interactions between membrane and secretory proteins. Their conformational maturation is assisted by a vast array of chaperones and enzymes, ensuring the fidelity of intercellular communication. These folding assistants reside in the early secretory compartment (ESC), a functional unit that encompasses endoplasmic reticulum (ER), intermediate compartment and cis-Golgi. Most soluble ESC residents have C-terminal KDEL-like motifs that prevent their transport beyond the Golgi. However, some accumulate in the ER, while others in downstream stations, implying different recycling rates. Moreover, it is now clear that cells can actively secrete certain ESC residents but not others. This essay discusses the physiology of their differential intracellular distribution, and the mechanisms that may ensure selectivity of release.https://www.frontiersin.org/articles/10.3389/fcell.2022.967875/fullKDEL receptorsprotein quality controlprotein secretionERp44PDIprotein folding
spellingShingle F. C. Palazzo
R. Sitia
T. Tempio
Selective Secretion of KDEL-Bearing Proteins: Mechanisms and Functions
Frontiers in Cell and Developmental Biology
KDEL receptors
protein quality control
protein secretion
ERp44
PDI
protein folding
title Selective Secretion of KDEL-Bearing Proteins: Mechanisms and Functions
title_full Selective Secretion of KDEL-Bearing Proteins: Mechanisms and Functions
title_fullStr Selective Secretion of KDEL-Bearing Proteins: Mechanisms and Functions
title_full_unstemmed Selective Secretion of KDEL-Bearing Proteins: Mechanisms and Functions
title_short Selective Secretion of KDEL-Bearing Proteins: Mechanisms and Functions
title_sort selective secretion of kdel bearing proteins mechanisms and functions
topic KDEL receptors
protein quality control
protein secretion
ERp44
PDI
protein folding
url https://www.frontiersin.org/articles/10.3389/fcell.2022.967875/full
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