What question did this study set out to answer?

To determine how yeast cells coordinate surface membrane assembly and secretion by tracking the synthesis and export of plasma membrane ATPase.

March 1, 1988The Journal of Cell BiologyOpen Access

Secretory vesicles externalize the major plasma membrane ATPase in yeast.

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Authors

CHCherie L. HolcombUniversity of Geneva WHWilliam J. HansenWorcester State University TETomás EtcheverryUniversity of Buenos Aires

Discussion

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Overview

Biochemical analysis demonstrates co-transport of plasma membrane ATPase and acid phosphatase in secretory vesicles in yeast, indicating shared pathways for membrane assembly and secretion.

Key Points

To determine how yeast cells coordinate surface membrane assembly and secretion by tracking the synthesis and export of plasma membrane ATPase.
Analyzed the biogenesis and transit of plasma membrane ATPase across secretion-defective (sec) mutant strains of Saccharomyces cerevisiae.
Biochemically characterized Golgi-derived secretory vesicles that accumulate in sec1 mutants blocked at the final secretory step.
Identified PM ATPase as a ~106-kD polypeptide exported via the secretory pathway without detectable asparagine-linked glycosylation or proteolytic modification.
Demonstrated that accumulated vesicles in sec1 mutants co-transport both PM ATPase and the soluble secretory enzyme acid phosphatase within the same vesicle species.

Cite This Study

Holcomb et al. (1988) studied this question.

synapsesocial.com/papers/6a72bb3df44fa9f079e01b1a https://doi.org/10.1083/jcb.106.3.641

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March 1, 1988The Journal of Cell BiologyOpen Access

Secretory vesicles externalize the major plasma membrane ATPase in yeast.

View Full Paper

Ask AI

Bookmark

Authors

CHCherie L. HolcombUniversity of Geneva WHWilliam J. HansenWorcester State University TETomás EtcheverryUniversity of Buenos Aires

Discussion

Member takes

Overview

Biochemical analysis demonstrates co-transport of plasma membrane ATPase and acid phosphatase in secretory vesicles in yeast, indicating shared pathways for membrane assembly and secretion.

Key Points

To determine how yeast cells coordinate surface membrane assembly and secretion by tracking the synthesis and export of plasma membrane ATPase.
Analyzed the biogenesis and transit of plasma membrane ATPase across secretion-defective (sec) mutant strains of Saccharomyces cerevisiae.
Biochemically characterized Golgi-derived secretory vesicles that accumulate in sec1 mutants blocked at the final secretory step.
Identified PM ATPase as a ~106-kD polypeptide exported via the secretory pathway without detectable asparagine-linked glycosylation or proteolytic modification.
Demonstrated that accumulated vesicles in sec1 mutants co-transport both PM ATPase and the soluble secretory enzyme acid phosphatase within the same vesicle species.

Cite This Study

Holcomb et al. (1988) studied this question.

synapsesocial.com/papers/6a72bb3df44fa9f079e01b1a https://doi.org/10.1083/jcb.106.3.641

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