The α- and β′-COP WD40 Domains Mediate Cargo-selective Interactions with Distinct Di-lysine Motifs

Eugster, Anne; Frigerio, Gabriella; Dale, Martin; Duden, Rainer

doi:10.1091/mbc.e03-10-0724

Cited by 102 publications

(122 citation statements)

References 48 publications

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“…3C). Cargo-specific functions for the COPI coat have been described previously in yeast (21)(22)(23). Importantly, it shows that ␤-COP depletion does not produce general cell death.…”

Section: Down-regulation Of ␤-Cop Protein Expression In Ht-29cl19asupporting

confidence: 68%

Cystic Fibrosis Transmembrane Conductance Regulator Trafficking Is Mediated by the COPI Coat in Epithelial Cells

Rennolds

Tower

Musgrove

et al. 2008

Journal of Biological Chemistry

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Cystic fibrosis (CF) is caused by defects in the CF transmembrane conductance regulator (CFTR) that functions as a chloride channel in epithelial cells. The most common cause of CF is the abnormal trafficking of CFTR mutants. Therefore, understanding the cellular machineries that transit CFTR from the endoplasmic reticulum to the plasma membrane (PM) is important. The coat protein complex I (COPI) has been implicated in the anterograde and retrograde transport of proteins and lipids between the endoplasmic reticulum and the Golgi. Here, we investigated the role of COPI in CFTR trafficking. Blocking COPI recruitment to membranes by expressing an inactive form of the GBF1 guanine nucleotide exchange factor for ADP-ribosylation factor inhibits CFTR trafficking to the PM. Similarly, inhibiting COPI dissociation from membranes by expressing a constitutively active ADP-ribosylation factor 1 mutant arrests CFTR within disrupted Golgi elements. To definitively explore the relationship between COPI and CFTR in epithelial cells, we depleted ␤-COP from the human colonic epithelial cell HT-29Cl.19A using small interfering RNA. ␤-COP depletion did not affect CFTR synthesis but impaired its trafficking to the PM. The arrest occurred pre-Golgi as shown by reduced level of glycosylation. Importantly, decreased trafficking of CFTR had a functional consequence as cells depleted of ␤-COP showed decreased cAMP-activated chloride currents. To explore the mechanism of COPI action in CFTR traffic we tested whether CFTR was COPI cargo. We discovered that the ␣-, ␤-, and ␥-subunits of COPI co-immunoprecipitated with CFTR. Our results indicate that the COPI complex plays a critical role in CFTR trafficking to the PM.

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“…3C). Cargo-specific functions for the COPI coat have been described previously in yeast (21)(22)(23). Importantly, it shows that ␤-COP depletion does not produce general cell death.…”

Section: Down-regulation Of ␤-Cop Protein Expression In Ht-29cl19asupporting

confidence: 68%

Cystic Fibrosis Transmembrane Conductance Regulator Trafficking Is Mediated by the COPI Coat in Epithelial Cells

Rennolds

Tower

Musgrove

et al. 2008

Journal of Biological Chemistry

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“…The following antibodies (Abs) were used: polyclonal Ab (pAb) against human GM130 and giantin (Marra et al, 2001); pAb against ␥-subunit of plant (Arabidopsis thaliana) COP-I (Pimpl et al, 2000); pAbs against different subunits of mammalian, yeast and plant COP-I from: F. Wieland, Heidelberg University, Germany (Faulstich et al, 1996); D. Robinson, Heidelberg University, Germany (Pimpl et al, 2000); M. Krieger, Massachusetts Institute of Technology, Cambridge, MA (Guo et al, 1994); R. Duden, University of Cambridge, Cambridge, UK (Eugster et al, 2004); S. Coughlan, Agilent Technologies, Wilmington, DE (Pimpl et al, 2000). Abs against P. grylli structural proteins of spore wall and polar tube (p40 and PTP A, see below) were generated and purified as described previously (Dolgikh et al, 2005).…”

Section: Antibodiesmentioning

confidence: 99%

Analogs of the Golgi complex in microsporidia: structure and avesicular mechanisms of function

Beznoussenko

Dolgikh

Seliverstova

et al. 2007

Journal of Cell Science

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Microsporidia are obligatory intracellular parasites, most species of which live in the host cell cytosol. They synthesize and then transport secretory proteins from the endoplasmic reticulum to the plasma membrane for formation of the spore wall and the polar tube for cell invasion. However, microsporidia do not have a typical Golgi complex. Here, using quick-freezing cryosubstitution and chemical fixation, we demonstrate that the Golgi analogs of the microsporidia Paranosema (Antonospora) grylli and Paranosema locustae appear as 300-nm networks of thin (25- to 40-nm diameter), branching or varicose tubules that display histochemical features of a Golgi, but that do not have vesicles. Vesicles are not formed even if membrane fusion is inhibited. These tubular networks are connected to the endoplasmic reticulum, the plasma membrane and the forming polar tube, and are positive for Sec13, γCOP and analogs of giantin and GM130. The spore-wall and polar-tube proteins are transported from the endoplasmic reticulum to the target membranes through these tubular networks, within which they undergo concentration and glycosylation. We suggest that the intracellular transport of secreted proteins in microsporidia occurs by a progression mechanism that does not involve the participation of vesicles generated by coat proteins I and II.

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“…Various subsets of dilysine motifs exist that are recognized differentially by the coatomer complex (SchroderKohne et al 1998). In contrast to the p24 familiy carboxy-terminal signatures, KKXX motifs interact with the WD40 domain of a-COP, and KXKXX binds to a similar domain within b 0 -COP (Eugster et al 2004). Thus structural differences constitute the molecular basis for coatomer to discriminate machinery components that are recycled from cargo proteins that are transported and delivered unidirectionally.…”

Section: Cargo Sorting/sorting Motifsmentioning

confidence: 99%

COPI Budding within the Golgi Stack

Popoff

Adolf²,

Brügger³

et al. 2011

Cold Spring Harbor Perspectives in Biology

152

169

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The Golgi serves as a hub for intracellular membrane traffic in the eukaryotic cell. Transport within the early secretory pathway, that is within the Golgi and from the Golgi to the endoplasmic reticulum, is mediated by COPI-coated vesicles. The COPI coat shares structural features with the clathrin coat, but differs in the mechanisms of cargo sorting and vesicle formation. The small GTPase Arf1 initiates coating on activation and recruits en bloc the stable heptameric protein complex coatomer that resembles the inner and the outer shells of clathrin-coated vesicles. Different binding sites exist in coatomer for membrane machinery and for the sorting of various classes of cargo proteins. During the budding of a COPI vesicle, lipids are sorted to give a liquid-disordered phase composition. For the release of a COPI-coated vesicle, coatomer and Arf cooperate to mediate membrane separation.

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The α- and β′-COP WD40 Domains Mediate Cargo-selective Interactions with Distinct Di-lysine Motifs

Cited by 102 publications

References 48 publications

Cystic Fibrosis Transmembrane Conductance Regulator Trafficking Is Mediated by the COPI Coat in Epithelial Cells

Cystic Fibrosis Transmembrane Conductance Regulator Trafficking Is Mediated by the COPI Coat in Epithelial Cells

Analogs of the Golgi complex in microsporidia: structure and avesicular mechanisms of function

COPI Budding within the Golgi Stack

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