Golgi complex–plasma membrane trafficking directed by an autonomous, tribasic Golgi export signal

Parmar, Hirendrasinh B.; Barry, Christopher; Kai, FuiBoon; Duncan, Roy

doi:10.1091/mbc.e13-07-0364

Cited by 32 publications

(39 citation statements)

References 64 publications

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“…While in general the deletion of these signals leads to the apical or nonpolarized distribution of the protein, it has also been reported to induce the retention of the protein in the Golgi apparatus in several cases . Thus, the mutation of a membrane proximal tribasic motif in the reovirus p14 fusion‐associated small transmembrane (FAST) protein was associated with the accumulation of the protein in the TGN . Similarly, the mutation of the Golgi export signals of the potassium channel Kir2.1 that is formed by a patch of residues present in the tertiary structure of the protein leads to the intracellular accumulation of the protein in the Golgi.…”

Section: Discussionmentioning

confidence: 70%

Role of the cytosolic domain of occludin in trafficking and hepatitis C virus infection

Lavie

Linna

Moustafa

et al. 2019

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The role of the tight‐junction (TJ) protein occludin (OCLN) in hepatitis C virus (HCV) entry remains elusive. Here, we investigated the OCLN C‐terminal cytosolic domain in HCV infection. We expressed a series of C‐terminal deletion mutants in Huh‐7 cells KO for OCLN and characterized their functionality in HCV infection and trafficking. Deleting the OCLN cytosolic domain led to protein instability and intracellular retention. The first 15 residues (OCLN‐C15 mutant) of the cytosolic domain were sufficient for OCLN stability, but led to its accumulation in the trans‐Golgi network (TGN) due to a deficient cell surface export after synthesis. In contrast, the OCLN‐C18 mutant, containing the first 18 residues of the cytosolic domain, was expressed at the cell surface and could mediate HCV infection. Point mutations in the context of C18 showed that I279 and W281 are crucial residues for cell surface expression of OCLN‐C18. However, in the context of full‐length OCLN, mutation of these residues only partially affected infection and cell surface localization. Importantly, the characterization of OCLN‐C18 in human‐polarized hepatocytes revealed a defect in its TJ localization without affecting HCV infection. These data suggest that TJ localization of OCLN is not a prerequisite for HCV infection in polarized hepatocytes.

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Section: Discussionmentioning

confidence: 70%

Role of the cytosolic domain of occludin in trafficking and hepatitis C virus infection

Lavie

Linna

Moustafa

et al. 2019

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“…These differences in acylation may affect functionality. Based on apparent mislocalization of NSP1-1, it is possible that signals that mediate trafficking from the endoplasmic reticulum, where FAST proteins are translated, to the plasma membrane, via the secretory pathway (38, 44-47), fail to function appropriately in some non-homologous hosts. Chimeric FAST proteins containing individual domain exchanges between RVB Bang117 NSP1-1 and NBV p10, similar to those engineered by Eileen Clancy for other FAST proteins (30, 31, 48), may provide insight into protein domains responsible for the species-specific fusion activity of RVB Bang117 NSP1-1.…”

Section: Discussionmentioning

confidence: 99%

Group B rotavirus encodes a functional fusion-associated small transmembrane (FAST) protein

Diller

Parrington

Patton

et al. 2019

Preprint

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word count: 243 19 Text word count: 6,601 20 21 2 ABSTRACT 22Rotavirus is an important cause of diarrheal disease in young mammals. Group A 23 rotavirus (RVA) causes most human rotavirus diarrheal disease and primarily affects 24 infants and young children. Group B rotavirus (RVB) has been associated with sporadic 25 outbreaks of human adult diarrheal disease. RVA and RVB are predicted to encode 26 mostly homologous proteins but differ significantly in the proteins encoded by the NSP1 27 gene. In the case of RVB, the NSP1 gene encodes two putative protein products of 28 unknown function, NSP1-1 and NSP1-2. We demonstrate that human RVB NSP1-1 29 mediates syncytia formation in cultured human cells. Based on sequence alignment, 30 NSP1-1 from groups B, G, and I contain features consistent with fusion-associated 31 small transmembrane (FAST) proteins, which have previously been identified in other 32Reoviridae viruses. Like some other FAST proteins, RVB NSP1-1 is predicted to have 33 an N-terminal myristoyl modification. Addition of an N-terminal FLAG peptide disrupts 34 NSP1-1-mediated fusion, consistent with a role for this fatty-acid modification in NSP1-1 35 function. NSP1-1 from a human RVB mediates fusion of human cells but not hamster 36 cells and, thus, may serve as a species tropism determinant. NSP1-1 also can enhance 37 RVA replication in human cells, both in single-cycle infection studies and during a multi-38 cycle time course in the presence of fetal bovine serum, which inhibits rotavirus spread. 39These findings suggest potential yet untested roles for NSP1-1 in RVB species tropism, 40 immune evasion, and pathogenesis. 41 42

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“…As a cisterna matures from the carbohydrate synthesis stage to the carrier formation stage, it receives peripheral and transmembrane TGN proteins from maturing TGN cisternae [5, 93 ••]. Moreover, mutant forms of some plasma membrane proteins accumulate in the TGN [94, 95 •], consistent with the existence of active recycling from older to younger TGN cisternae. Such a recycling pathway could explain why secretory proteins exit the Golgi with exponential rather than linear kinetics [10].…”

Section: From the Golgi: The Carrier Formation Stagementioning

confidence: 99%

Golgi compartmentation and identity

Papanikou

Glick

2014

Current Opinion in Cell Biology

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Recent work supports the idea that cisternae of the Golgi apparatus can be assigned to three classes, which correspond to discrete stages of cisternal maturation. Each stage has a unique pattern of membrane traffic. At the first stage, cisternae form in association with the ER at multifunctional membrane assembly stations. At the second stage, cisternae synthesize carbohydrates while exchanging material via COPI vesicles. At the third stage, cisternae of the trans-Golgi network segregate into domains and produce transport carriers with the aid of specific lipids and the actin cytoskeleton. These processes are coordinated by cascades of Rab and Arf/Arl GTPases.

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Golgi complex–plasma membrane trafficking directed by an autonomous, tribasic Golgi export signal

Cited by 32 publications

References 64 publications

Role of the cytosolic domain of occludin in trafficking and hepatitis C virus infection

Role of the cytosolic domain of occludin in trafficking and hepatitis C virus infection

Group B rotavirus encodes a functional fusion-associated small transmembrane (FAST) protein

Golgi compartmentation and identity

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