beta′-COP, a novel subunit of coatomer.

Stenbeck, Gudrun; Harter, Cordula; Brecht, Andreas; Herrmann, Doris; Lottspeich, Friedrich; Orci, Lelio; Wieland, Felix

doi:10.1002/j.1460-2075.1993.tb05945.x

Cited by 107 publications

(78 citation statements)

References 35 publications

(12 reference statements)

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“…COPI is a seven-subunit complex involved in both intra-Golgi and Golgi-to-ER vesicle-mediated trafficking (18,19). We noticed that Ist2ct harbors a "KKXX-like motif" known to interact with COPI that promotes cargo retrieval from the Golgi to the ER (20).…”

Section: Resultsmentioning

confidence: 99%

Induction of cortical endoplasmic reticulum by dimerization of a coatomer-binding peptide anchored to endoplasmic reticulum membranes

Lavieu

Orci²,

Shi

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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Cortical endoplasmic reticulum (cER) is a permanent feature of yeast cells but occurs transiently in most animal cell types. Ist2p is a transmembrane protein that permanently localizes to the cER in yeast. When Ist2 is expressed in mammalian cells, it induces abundant cER containing Ist2. Ist2 cytoplasmic C-terminal peptide is necessary and sufficient to induce cER. This peptide sequence resembles classic coat protein complex I (COPI) coatomer protein-binding KKXX signals, and indeed the dimerized peptide binds COPI in vitro. Controlled dimerization of this peptide induces cER in cells. RNA interference experiments confirm that coatomer is required for cER induction in vivo, as are microtubules and the microtubule plus-end binding protein EB1. We suggest that Ist2 dimerization triggers coatomer binding and clustering of this protein into domains that traffic at the microtubule growing plus-end to generate the cER beneath the plasma membrane. Sequences similar to the Ist2 lysine-rich tail are found in mammalian STIM proteins that reversibly induce the formation of cER under calcium control

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Section: Resultsmentioning

confidence: 99%

Induction of cortical endoplasmic reticulum by dimerization of a coatomer-binding peptide anchored to endoplasmic reticulum membranes

Lavieu

Orci²,

Shi

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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“…For Western blot analyses, the antipeptide antibodies C1PL (␤Ј-COP) (35,36) and ARF1-C1 were used. The ARF1-C1 antibody is directed against the C-terminal ARF1 sequence CDWLSNQLRNQK that was coupled to keyhole limpet hemocyanin using glutaraldehyde crosslinking.…”

Section: Methodsmentioning

confidence: 99%

Functional reconstitution of COPI coat assembly and disassembly using chemically defined components

Reinhard

Schweikert

Wieland

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

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Coat protein I (COPI)-coated transport vesicles mediate protein and lipid transport in the early secretory pathway. The basic machinery required for the formation of these transport intermediates has been elucidated based on the reconstitution of COPI-coated vesicle formation from chemically defined liposomes. In this experimental system, the coat components coatomer and GTP-bound ADPribosylation factor (ARF), as well as p23 as a membrane-bound receptor for COPI coat proteins, were shown to be both necessary and sufficient to promote COPI-coated vesicle formation. coatomer ͉ ADP-ribosylation factor ͉ ARF-GAP ͉ p24 protein family

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“…In the following, we focus on RACK1, the selective RACK for bIIPKC (Ron et al, 1994), and RACK2 (previously identi®ed as b`COP' (Harrison-Lavoie et al, 1993;Stenbeck et al, 1993)), the selective RACK for ePKC (Csukai et al, 1997). Both RACKs contain seven repeats of the WD40 motif, ®rst identi®ed in the b subunit of the heterotrimeric G protein, Gb (Fong et al, 1987).…”

Section: Speci®city Of Pkc-mediated Signaling Is Provided By Anchorinmentioning

confidence: 99%

Adaptor proteins in protein kinase C-mediated signal transduction

2001

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Spatial and temporal organization of signal transduction is essential in determining the speed and precision by which signaling events occur. Adaptor proteins are key to organizing signaling enzymes near their select substrates and away from others in order to optimize precision and speed of response. Here, we describe the role of adaptor proteins in determining the speci®c function of individual protein kinase C (PKC) isozymes. These isozymeselective proteins were called collectively RACKs (receptors for activated C-kinase). The role of RACKs in PKC-mediated signaling was determined using isozyme-speci®c inhibitors and activators of the binding of each isozyme to its respective RACK. In addition to anchoring activated PKC isozymes, RACKs anchor other signaling enzymes. RACK1, the anchoring protein for activated bIIPKC, binds for example, Src tyrosine kinase, integrin, and phosphodiesterase. RACK2, the ePKC-speci®c RACK, is a coated-vesicle protein and thus is involved in vesicular release and cell ± cell communication. Therefore, RACKs are not only adaptors for PKC, but also serve as adaptor proteins for several other signaling enzymes. Because at least some of the proteins that bind to RACKs, including PKC itself, regulate cell growth, modulating their interactions with RACKs may help elucidate signaling pathways leading to carcinogenesis and could result in the identi®cation of novel therapeutic targets. Oncogene (2001) 20, 6339 ± 6347.

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beta′-COP, a novel subunit of coatomer.

Cited by 107 publications

References 35 publications

Induction of cortical endoplasmic reticulum by dimerization of a coatomer-binding peptide anchored to endoplasmic reticulum membranes

Induction of cortical endoplasmic reticulum by dimerization of a coatomer-binding peptide anchored to endoplasmic reticulum membranes

Functional reconstitution of COPI coat assembly and disassembly using chemically defined components

Adaptor proteins in protein kinase C-mediated signal transduction

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