Fission yeast and a plant have functional homologues of the Sar1 and Sec12 proteins involved in ER to Golgi traffic in budding yeast.

d’Enfert, Christophe; Gensse, Marc; Gaillardin, Claude

doi:10.1002/j.1460-2075.1992.tb05514.x

Cited by 119 publications

(67 citation statements)

References 45 publications

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“…The uncoating of the vesicles relies on Sarlp GTP hydrolysis, a necessary step in targeting and fusion of the vesicles to the acceptor compartment (Barlowe et al, 1994). Homologues of some COPII components (Sarlp, Secl3p, Secl2p) have been identified in plants and mammals (Orci et al, 1991;d'Enfert et al, 1992;Kuge et al, 1994).…”

Section: Introductionmentioning

confidence: 99%

Cloning and functional characterization of mammalian homologues of the COPII component Sec23.

Paccaud

Reith

Carpentier

et al. 1996

MBoC

107

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We screened a human cDNA library with a probe derived from a partial SEC23 mouse homologue and isolated two different cDNA clones (hSec23A and hSec23B) encoding proteins of a predicted molecular mass of 85 kDa. hSec23Ap and hSec23Bp were 85% identical and shared 48% identity with the yeast Sec23p. Affinity-purified anti-hSec23A recognized a protein of -85 kDa on immunoblots of human, mouse, and rat cell extracts but did not recognize yeast Sec23p. Cytosolic hSec23Ap migrated with an apparent molecular weight of 350 kDa on a gel filtration column, suggesting that it is part of a protein complex. By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. hSec23Ap is a functional homologue of the yeast Sec23p as the hSec23A isoform complemented the temperature sensitivity of the Saccharomyces cerevisiae sec23-1 mutation at a restrictive temperature of 34°C. RNase protection assays indicated that both hSec23 isoforms are coexpressed in various human tissues, although at a variable ratio. Our data demonstrate that hSec23Ap is the functional human counterpart of the yeast COPII component Sec23p and suggest that it plays a similar role in mammalian protein export from the ER. The exact function of hSec23Bp remains to be determined.

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Section: Introductionmentioning

confidence: 99%

Cloning and functional characterization of mammalian homologues of the COPII component Sec23.

Paccaud

Reith

Carpentier

et al. 1996

MBoC

107

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“…However, proteins with analogous functions have not yet been identified in plants. Plant homologs of components of the COPI and COPII vesicle coats have been identified and some characterization studies have been carried out (d'Enfert et al, 1992;Regad et al, 1993;Bar-Peled and Raikhel, 1997;Takeuchi et al, 1998;Movafeghi et al, 1999;Contreras et al, 2000;Pimpl et al, 2000;Vernoud et al, 2003;daSilva et al, 2004;Yang et al, 2005;Stefano et al, 2006). Although this area of research is currently one of great interest and activity, knowledge of transport in the early secretory pathway of plants still lags behind that from yeast and mammalian systems.…”

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confidence: 99%

De Novo Formation of Plant Endoplasmic Reticulum Export Sites Is Membrane Cargo Induced and Signal Mediated

et al. 2007

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The plant endoplasmic reticulum (ER) contains functionally distinct subdomains at which cargo molecules are packed into transport carriers. To study these ER export sites (ERES), we used tobacco (Nicotiana tabacum) leaf epidermis as a model system and tested whether increased cargo dosage leads to their de novo formation. We have followed the subcellular distribution of the known ERES marker based on a yellow fluorescent protein (YFP) fusion of the Sec24 COPII coat component (YFP-Sec24), which, differently from the previously described ERES marker, tobacco Sar1-YFP, is visibly recruited at ERES in both the presence and absence of overexpressed membrane cargo. This allowed us to quantify variation in the ERES number and in the recruitment of Sec24 to ERES upon expression of cargo. We show that increased synthesis of membrane cargo leads to an increase in the number of ERES and induces the recruitment of Sec24 to these ER subdomains. Soluble proteins that are passively secreted were found to leave the ER with no apparent up-regulation of either the ERES number or the COPII marker, showing that bulk flow transport has spare capacity in vivo. However, de novo ERES formation, as well as increased recruitment of Sec24 to ERES, was found to be dependent on the presence of the diacidic ER export motif in the cytosolic domain of the membrane cargo. Our data suggest that the plant ER can adapt to a sudden increase in membrane cargo-stimulated secretory activity by signal-mediated recruitment of COPII machinery onto existing ERES, accompanied by de novo generation of new ERES.

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“…These COPII components are highly conserved across species, [11][12][13][14][15][16][17] including plants. 12,[18][19][20] Here, we report the isolation and expression analysis of two Arabidopsis thaliana homologs of Sec13, the AtSec13A and AtSec13B genes.…”

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confidence: 99%

“…12,[18][19][20] Here, we report the isolation and expression analysis of two Arabidopsis thaliana homologs of Sec13, the AtSec13A and AtSec13B genes. We detected the interaction of AtSec13A and AtSec13B with an A. thaliana Sec31 homolog (AtSec31A).…”

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confidence: 99%

Two Sec13p Homologs, AtSec13A and AtSec13B, Redundantly Contribute to the Formation of COPII Transport Vesicles inArabidopsis thaliana

Hino

Tanaka

Kawamukai

et al. 2011

Bioscience, Biotechnology, and Biochemistry

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Fission yeast and a plant have functional homologues of the Sar1 and Sec12 proteins involved in ER to Golgi traffic in budding yeast.

Cited by 119 publications

References 45 publications

Cloning and functional characterization of mammalian homologues of the COPII component Sec23.

Cloning and functional characterization of mammalian homologues of the COPII component Sec23.

De Novo Formation of Plant Endoplasmic Reticulum Export Sites Is Membrane Cargo Induced and Signal Mediated

Two Sec13p Homologs, AtSec13A and AtSec13B, Redundantly Contribute to the Formation of COPII Transport Vesicles inArabidopsis thaliana

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