The evolving understanding of COPI vesicle formation

Hsu, Victor; Lee, Stella Y.; Yang, Jia‐Shu

doi:10.1038/nrm2663

Cited by 70 publications

(68 citation statements)

References 65 publications

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“…It is possible that Arf1•GTPgS could slow coatomer polymerization, implying a mechanism in which release of Arf1•GTP is required to ensure that cargo associates with coatomer prior to coatomer polymerization. This interpretation is consistent with the results reported by Hsu and colleagues 35,36,68 in which they found that the [R50K] ArfGAP1 did not efficiently generate COPI vesicles.…”

Section: Discussionsupporting

confidence: 83%

ArfGAP1 promotes COPI vesicle formation by facilitating coatomer polymerization

et al. 2011

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Section: Discussionsupporting

confidence: 83%

ArfGAP1 promotes COPI vesicle formation by facilitating coatomer polymerization

et al. 2011

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“…COPI, which is among the best-characterized coat complexes, is a cytosolic complex that coats Golgi-derived vesicles and is involved in protein transport from the Golgi apparatus to the endoplasmic reticulum via recruitment by Arf1. [21][22][23] Although the precise cellular mechanisms of COPI, and circulating COPE-Ab, in patients with OSA were not revealed by the current study, lipid inflammation might be a key element associated with elevated COPE-Ab levels in this patient population. Previous studies have reported that the Arf1-COPI vesicular transport machinery regulates droplet morphology and lipid storage/utilization within the vesicle-trafficking pathway.…”

Section: 16mentioning

confidence: 75%

Circulating Anti-Coatomer Protein Complex Subunit Epsilon (COPE) Autoantibodies as a Potential Biomarker for Cardiovascular and Cerebrovascular Events in Patients with Obstructive Sleep Apnea

Matsumura

Terada

Kinoshita

et al. 2017

Journal of Clinical Sleep Medicine

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Study Objectives: Although moderate to severe obstructive sleep apnea (OSA) is an independent risk factor for severe arteriosclerotic diseases such as cardiovascular disease (CVD) and stroke, the development of atherosclerosis-related diseases cannot yet be predicted in patients with OSA. In a pilot study, we identified autoantibodies against the coatomer protein complex, subunit epsilon [circulating anti-coatomer protein complex subunit epsilon autoantibody (COPE-Ab)], a cytosolic complex that mediates protein transport in the Golgi compartment, as a potential novel biomarker of atherosclerosis. This study aimed to evaluate whether COPE-Ab levels had an association with cardiovascular and cerebrovascular events in patients with OSA. Methods: Eighty-two adult patients with a diagnosis of OSA via polysomnography and 64 healthy donors were studied. Serum COPE-Ab levels were measured using an amplified luminescence proximity homogeneous assay. Then, clinical factors related to atherosclerosis were evaluated with respect to COPE-Ab levels. Results: Significant differences in COPE-Ab levels were observed in terms of OSA severity. COPE-Ab levels were significantly higher in patients with OSA and also CVD and/or stroke, hypertension, and a high body mass index. Univariate and multivariate logistic regression analyses of patients with OSA identified elevated COPE-Ab level as a significant predictor of CVD and/or stroke. Conclusions: An elevated COPE-Ab level may be a potential predictor of the risks of cardiovascular and cerebrovascular events in patients with OSA. Therefore, patients with higher COPE-Ab levels may require more careful and intensive treatment. Commentary: A commentary on this article appears in this issue on page 361.

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“…In cell assays, brefeldin disrupts the Golgi complex, in part by ADP-ribosylating a protein called BARS (brefeldin A ADP-ribosylated substrate) which is necessary for vesicle fission (91). However, in a rat brain model, brefeldin did not directly act on BARS but was first endowed with an ADP-ribose moiety provided by CD38 (92), opening an exciting new avenue of research into the possible therapeutic uses of brefeldin in CD38 hi tumor cells.…”

Section: Connections No 2: Arcs and Other Nad-consuming Enzymesmentioning

confidence: 99%

The ADP-ribosyl cyclases - the current evolutionary state of the ARCs

et al. 2014

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The major ADP-ribosylating enzyme families are the focus of this special issue of Frontiers in Bioscience. However, there is room for another family of enzymes with the capacity to utilize nicotinamide adenine dinucleotide (NAD): the ADPribosyl cyclases (ARCs). These unique enzymes catalyse the cyclization of NAD to cyclic ADP ribose (cADPR), a widely distributed second messenger. However, the ARCs are versatile enzymes that can manipulate NAD, NAD phosphate (NADP) and other substrates to generate various bioactive molecules including nicotinic acid adenine dinucleotide diphosphate (NAADP) and ADP ribose (ADPR). This review will focus on the group of well-characterized ARCs identified in invertebrate and vertebrate animals, whose common gene structure allows us to trace their origin to the ancestor of bilaterian animals. Behind a façade of gene and protein homology lies a family with a disparate functional repertoire dictated by the animal model and the physical trait under investigation. Here we present a phylogenetic view of the ARCs to better understand the evolution of function in this family. Eggs, this "rich source for experimentation" have been a cornucopia for the ARCs. It was in the egg of the sea urchin Lytechinus pictus that cADPR was first identified as a mediator of stimulus-induced calcium release (2). It was another invertebrate egg, that of the sea slug Aplysia californica, that gave us the first enzyme capable of cADPR biosynthesis (3). Here is the story in brief. INTRODUCTIONThe excitement began just over 25 years ago when it first emerged that NAD, NADP and then cADPR could trigger Ca 2+ release in eggs of the sea urchin Lytechinus pictus (4), on a par with inositol-1,4,5-trisphosphate (InsP3) (5), until then one of the most potent intracellular messengers. Although the capacity to synthesize cADPR and mobilize Ca 2+ was shown to be quite broadly distributed in animal tissues (6), the enzyme responsible for converting NAD to cADPR remained unknown. By a classic 2 stroke of serendipity, the enzyme was detected by scientists studying ADP-ribosylation of G-proteins by the bacterial cholera and diptheria exotoxins in the marine gastropod mollusc Aplysia californica (7). ADP-ribosylation occurred in all examined tissues, except in the ovotestis. The unexpected finding was intelligently pursued until the 'inhibitory factor' was characterized as a NADsplitting protein capable of producing cADPR, similar to the enzymatic activity first identified in sea urchin eggs. This first ARC was molecularly cloned (8) and called 'ADP-ribosyl cyclase' in 1991 by Lee and Aarhus to avoid confusion with other NAD glycohydrolases (EC 3.2.2.5) (3). As will be discussed below, the antagonism between the mono-ADP-ribosyltransferases (mART) and the ARCs revealed in molluscan eggs is probably just the tip of the iceberg of this phenomenon. In the meantime, the availability of an amino acid sequence enabled the sequence homology-based identification of ARCs in other species, first amongst these, human CD38 (9). THE...

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The evolving understanding of COPI vesicle formation

Cited by 70 publications

References 65 publications

ArfGAP1 promotes COPI vesicle formation by facilitating coatomer polymerization

ArfGAP1 promotes COPI vesicle formation by facilitating coatomer polymerization

Circulating Anti-Coatomer Protein Complex Subunit Epsilon (COPE) Autoantibodies as a Potential Biomarker for Cardiovascular and Cerebrovascular Events in Patients with Obstructive Sleep Apnea

The ADP-ribosyl cyclases - the current evolutionary state of the ARCs

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