Regulation of cargo export and sorting at the trans‐Golgi network

Martino, Rosaria Di; Sticco, Lucia; Luini, Alberto

doi:10.1002/1873-3468.13572

Cited by 63 publications

(51 citation statements)

References 104 publications

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“…Mutations in genes encoding for proteins involved in the trans-Golgi export machinery have been shown to cause severe genetic diseases [66,208]. For example, mutations in different subunits of the AP-1-complex, component of clathrin-coated vesicles and associated with the trans-Golgi and early/recycling endosomes, are linked with X-linked mental retardation and with MEDNIK syndrome (Mental retardation, Enteropathy, Deafness, peripheral Neuropathy, Ichthyosis and Keratodermia).…”

Section: J O U R N a L P R E -P R O O Fmentioning

confidence: 99%

Direct trafficking pathways from the Golgi apparatus to the plasma membrane

Stalder

Gershlick

2020

Seminars in Cell & Developmental Biology

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In eukaryotic cells, protein sorting is a highly regulated mechanism important for many physiological events. After synthesis in the endoplasmic reticulum and trafficking to the Golgi apparatus, proteins sort to many different cellular destinations including the endolysosomal system and the extracellular space. Secreted proteins need to be delivered directly to the cell surface. Sorting of secreted proteins from the Golgi apparatus has been a topic of interest for over thirty years, yet there is still no clear understanding of the machinery that forms the post-Golgi carriers. Most evidence points to these post-Golgi carriers being tubular pleomorphic structures that bud from the trans-face of the Golgi. In this review, we present the background studies and highlight the key components of this pathway, we then discuss the machinery implicated in the formation of these carriers, their translocation across the cytosol, and their fusion at the plasma membrane.Abbreviations: ATP, adenosine triphosphate; BFA, Brefeldin A; CARTS, CARriers of the TGN to the cell Surface; CI-MPR, cation-independent mannose-6 phosphate receptor; CtBP3/BARS, C-terminus binding protein 3/BFA adenosine diphosphate-ribosylated substrate; ER, endoplasmic reticulum; GlcCer, glucosylceramide; PAUF, pancreatic adenocarcinoma up-regulated factor; PM, plasma membrane; RUSH, retention using selective hooks; SBP, streptavidin-binding peptide; SM, sphingomyelin; SNARE, soluble N-ethylmaleimide sensitive fusion protein attachment protein receptor;SPCA1, secretory pathway calcium ATPase 1; TGN, trans-Golgi Network; TIRF, total internal reflection fluorescence; ts, temperature sensitive; VSV, vesicular stomatitis virus J o u r n a l P r e -p r o o f J o u r n a l P r e -p r o o f J o u r n a l P r e -p r o o f J o u r n a l P r e -p r o o f

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Section: J O U R N a L P R E -P R O O Fmentioning

confidence: 99%

Direct trafficking pathways from the Golgi apparatus to the plasma membrane

Stalder

Gershlick

2020

Seminars in Cell & Developmental Biology

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“…Many, perhaps most, cell biological processes involve proteins transitioning between cellular locations; evidence suggests that spatial regulation of the proteome is as important and extensive as regulation of protein abundance (1). Supporting this notion, an increasing number of diseases are associated with disturbances in protein localization (2)(3)(4). The ability to capture protein localization dynamics experimentally is hence key to understanding cellular physiology, and numerous methods for spatial proteomics are available.…”

Section: Organellar Maps Through Proteomic Profiling -mentioning

confidence: 99%

Organellar Maps Through Proteomic Profiling – A Conceptual Guide

Borner¹

2020

Molecular & Cellular Proteomics

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Protein subcellular localization is an essential and highly regulated determinant of protein function. Major advances in mass spectrometry and imaging have allowed the development of powerful spatial proteomics approaches for determining protein localization at the whole cell scale. Here, a brief overview of current methods is presented, followed by a detailed discussion of organellar mapping through proteomic profiling. This relatively simple yet flexible approach is rapidly gaining popularity, because of its ability to capture the localizations of thousands of proteins in a single experiment. It can be used to generate high-resolution cell maps, and as a tool for monitoring protein localization dynamics. This review highlights the strengths and limitations of the approach and provides guidance to designing and interpreting profiling experiments.

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“…Many secretory proteins require additional post-translational modifications in the form of glycosylation, phosphorylation, and protein cleavage in the Golgi Network (GN) to assume their final, active conformations (Potelle et al, 2015). After a secretory protein is fully synthesized and properly folded in the ER, it is exported to the cis-Golgi, commonly via the Coat Complex II (COP II) secretory vesicle pathway (Aridor et al, 1998), and ER escort chaperones are often packaged into the COP II vesicle together with their clients (Di Martino et al, 2019). In the cis-Golgi, secretory proteins may dissociate from the ER chaperone, potentially due to the more acidic pH of Golgi compartment compared to ER, and ultimately continue through the GN to undergo additional post-translational modifications and maturation (Gomez-Navarro and Miller, 2016).…”

Section: Introductionmentioning

confidence: 99%

The Probable, Possible, and Novel Functions of ERp29

et al. 2020

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The luminal endoplasmic reticulum (ER) protein of 29 kDa (ERp29) is a ubiquitously expressed cellular agent with multiple critical roles. ERp29 regulates the biosynthesis and trafficking of several transmembrane and secretory proteins, including the cystic fibrosis transmembrane conductance regulator (CFTR), the epithelial sodium channel (ENaC), thyroglobulin, connexin 43 hemichannels, and proinsulin. ERp29 is hypothesized to promote ER to cis-Golgi cargo protein transport via COP II machinery through its interactions with the KDEL receptor; this interaction may facilitate the loading of ERp29 clients into COP II vesicles. ERp29 also plays a role in ER stress (ERS) and the unfolded protein response (UPR) and is implicated in oncogenesis. Here, we review the vast array of ERp29's clients, its role as an ER to Golgi escort protein, and further suggest ERp29 as a potential target for therapies related to diseases of protein misfolding and mistrafficking.

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Regulation of cargo export and sorting at the trans‐Golgi network

Cited by 63 publications

References 104 publications

Direct trafficking pathways from the Golgi apparatus to the plasma membrane

Direct trafficking pathways from the Golgi apparatus to the plasma membrane

Organellar Maps Through Proteomic Profiling – A Conceptual Guide

The Probable, Possible, and Novel Functions of ERp29

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