@article{569,
title = {Reconstitution of protein transport using broken yeast spheroplasts},
author = { D Baker and R Schekman},
issn = {0091-679X},
year = {1989},
date = {1989-00-01},
journal = {Methods in Cell Biology},
volume = {31},
pages = {127-41},
keywords = {},
pubstate = {published},
tppubtype = {article}
}

@article{332,
title = {Reconstitution of SEC gene product-dependent intercompartmental protein transport},
author = { D Baker and L Hicke and M Rexach and M Schleyer and R Schekman},
url = {https://www.bakerlab.org/wp-content/uploads/2016/06/baker88.pdf},
issn = {0092-8674},
year = {1988},
date = {1988-07-01},
journal = {Cell},
volume = {54},
pages = {335-44},
abstract = {Transport of alpha-factor precursor from the endoplasmic reticulum to the Golgi apparatus has been reconstituted in gently lysed yeast spheroplasts. Transport is measured through the coupled addition of outer-chain carbohydrate to [35S]methionine-labeled alpha-factor precursor translocated into the endoplasmic reticulum of broken spheroplasts. The reaction is absolutely dependent on ATP, stimulated 6-fold by cytosol, and occurs between physically separable sealed compartments. Transport is inhibited by the guanine nucleotide analog GTP gamma S. sec23 mutant cells have a temperature-sensitive defect in endoplasmic reticulum-to-Golgi transport in vivo. This defect has been reproduced in vitro using sec23 membranes and cytosol. Transport at 30 degrees C with sec23 membranes requires addition of cytosol containing the SEC23 (wild-type) gene product. This demonstrates that an in vitro inter-organelle transport reaction depends on a factor required for transport in vivo. Complementation of sec mutations in vitro provides a functional assay for the purification of individual intercompartmental transport factors.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}

@article{333,
title = {Protein transport to the vacuole and receptor-mediated endocytosis by clathrin heavy chain-deficient yeast},
author = { G S Payne and D Baker and E van Tuinen and R Schekman},
url = {https://www.bakerlab.org/wp-content/uploads/2016/06/payne88A.pdf},
issn = {0021-9525},
year = {1988},
date = {1988-05-01},
journal = {The Journal of cell biology},
volume = {106},
pages = {1453-61},
abstract = {Clathrin heavy chain-deficient mutants (chcl) of Saccharomyces cerevisiae are viable but exhibit compromised growth rates. To investigate the role of clathrin in intercompartmental protein transport, two pathways have been monitored in chcl cells: transport of newly synthesized vacuolar proteins to the vacuole and receptor-mediated uptake of mating pheromone. Newly synthesized precursors of the vacuolar protease carboxypeptidase Y (CPY) were converted to mature CPY with similar kinetics in mutant and wild-type cells. chcl cells did not aberrantly secrete CPY and immunolocalization techniques revealed most of the CPY in chcl cells within morphologically identifiable vacuolar structures. Receptor-mediated internalization of the mating pheromone alpha-factor occurred in chcl cells at 36-50% wild-type levels. The mutant cells were fully competent to respond to pheromone-induced cell-cycle arrest. These results argue that in yeast, clathrin may not play an essential role either in vacuolar protein sorting and delivery or in receptor-mediated endocytosis of alpha-factor. Alternative mechanisms ordinarily may execute these pathways, or be activated in clathrin-deficient cells.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}